US11897929B2 - Compositions and methods for targeted cytokine delivery - Google Patents

Abstract

The present disclosure encompasses compositions and methods for targeted cytokine delivery. The compositions disclosed herein comprise a cytokine linked to an NKG2D ligand or PD1 ligand and may improve immunotherapy by limiting side effects associated with immunotherapy. The present disclosure also encompasses compositions and methods for recruiting cytotoxic lymphocytes to target cells using NKG2D receptor ligands or PD1 ligands. The compositions disclosed herein comprise a NKG2D receptor ligand and a targeting molecule and may improve immunotherapy by limiting side effects associated with immunotherapy.

Description

CROSS REFERENCE TO RELATED APPLICATIONS

This application claims the benefit of U.S. application Ser. No. 16/075,069, filed Aug. 2, 2018, PCT application number PCT/US2017/016688, filed Feb. 6, 2017, U.S. Provisional Application No. 62/292,046, filed Feb. 5, 2016, U.S. Provisional Application No. 62/342,630, filed May 27, 2016, U.S. Provisional Application No. 62/350,056, filed Jun. 14, 2016, and U.S. Provisional Application No. 62/419,146, filed Nov. 8, 2016, each of the disclosures of which is hereby incorporated by reference in its entirety.

GOVERNMENTAL RIGHTS

This invention was made with government support under AI073552, AI019687, AI109948, HHSN272201200026C and HL113931 awarded by the National Institutes of Health. The government has certain rights in the invention.

FIELD OF THE INVENTION

The present disclosure encompasses compositions and methods for targeted delivery of cytokines and for recruiting immune cells to target cells. Through specific delivery of cytokines and other agents, the compositions disclosed herein may improve immunotherapy and in some instances, limit side effects associated with immunotherapy.

BACKGROUND OF THE INVENTION

Systemic administration of high dose interleukin 2 (IL2) is one of the most potent forms of immunotherapy and is currently approved by the FDA for treatment of several malignancies. Efficacy of this treatment depends on activating cytotoxic lymphocytes (CTLs) such as natural killer cells (NK) and CD8⁺ T lymphocytes (CD8⁺ CTLs). Clinical trials have demonstrated approximately 15% partial or complete tumor responses, with up to 5% of patients having a durable long-lasting response resembling a cure. Despite these encouraging results in a minority of patients, most do not achieve a benefit or stop IL2 therapy prematurely due to complications such as blood pressure changes and pulmonary or systemic capillary leak. It is thought that the direct action of IL2 on vascular endothelium contributes to the majority of these side effects. The efficacy of IL2 is also limited by preferential activation of CD4⁺Foxp3+ regulatory T cells (T_regs), which decrease the tumor immune response. For these reasons treatment with high-dose IL2 has fallen out of favor clinically.

Side effects and deceased efficacy of IL2 therapy occur due to the high affinity trimeric αβγ IL2 receptor (IL2R), which is expressed by vascular endothelial cells and T_regs at baseline. Thus CD4⁺Foxp3⁺ T_regs and vascular endothelium are activated at much lower doses of IL2 than NK cells, which express the lower affinity βγ chains of the IL2R at rest. NK cells do express the high affinity α chain of IL2R after activation and depend on this trimeric receptor for peak cytolytic capacity. Mutant forms of IL2 with decreased affinity for IL2Rα have been described and offer a more favorable side effect profile. However, they also result in lower efficacy and decreased therapeutic potential due to decreased CTL activation. Therefore, there is a need in the art for a form of IL2 that could preferentially bind to and activate CTLs without activating T_regs and endothelial cells. Such an IL2 derivative might overcome such clinical barriers and result in more efficacious immunotherapy with fewer side effects.

SUMMARY OF THE INVENTION

In an aspect, the disclosure provides a composition comprising a cytokine linked to a NKG2D ligand. In one particular embodiment, the NKG2D ligand is an anti-NKG2D antibody.

In another aspect, the disclosure provides a composition comprising a ligand to the NKG2D receptor and a targeting molecule. The targeting molecule directs the composition to a binding partner on a target cell and recruits an immune cell upon the ligand specifically binding to the NKG2D receptor on the immune cell. In one instance, the ligand is orthopoxvirus major histocompatibility complex class I-like protein (OMCP). The targeting molecule can be linked to the ligand or unlinked and presented together in a single composition with the ligand or administered concurrently in separate compositions.

In another aspect, the disclosure provides a method to deliver a cytokine to a target cell comprising contacting a target cell with a composition comprising a cytokine linked to a NKG2D ligand. In still another aspect, the disclosure provides a method to activate immune cells comprising contacting an immune cell with a composition comprising a proinflammatory cytokine linked to a NKG2D ligand. The ligand specifically binds to a receptor on the immune cell thereby activating the cell.

In still another aspect, the disclosure provides a method to recruit and activate immune cells at a particular target cell comprising providing a composition comprising a ligand to an NKG2D receptor and a targeting molecule.

In still yet another aspect, the disclosure provides a method to treat a tumor comprising identifying a subject with a tumor and administering to the subject a therapeutically effective amount of a composition comprising a proinflammatory cytokine linked to a NKG2D ligand.

In a different aspect, the disclosure provides a method to treat a viral infection comprising administering to the subject a therapeutically effective amount of a composition comprising a proinflammatory cytokine linked to a NKG2D ligand. In other aspects, the disclosure provides a chimeric peptide comprising a cytokine peptide and a NKG2D ligand peptide.

In certain aspects, the disclosure provides a chimeric peptide comprising a cytokine peptide and an anti-NKG2D antibody.

In another aspect, the disclosure provides a composition comprising a cytokine linked to a programmed cell death protein 1 (PD1) ligand. In one particular embodiment, the PD1 ligand is programmed cell death ligand 1 (PDL1). In another particular embodiment, the PD1 ligand is programmed cell death ligand 2 (PDL2).

In another aspect, the disclosure provides a method to deliver a cytokine to a target cell comprising contacting a target cell with a composition comprising a cytokine linked to a PD1 ligand. In still another aspect, the disclosure provides a method to activate immune cells comprising contacting an immune cell with a composition comprising a proinflammatory cytokine linked to a PD1 ligand. The ligand specifically binds to a receptor on the immune cell thereby activating the cell.

In still yet another aspect, the disclosure provides a method to treat a tumor comprising identifying a subject with a tumor and administering to the subject a therapeutically effective amount of a composition comprising a proinflammatory cytokine linked to a PD1 ligand.

In a different aspect, the disclosure provides a method to treat a viral infection comprising administering to the subject a therapeutically effective amount of a composition comprising a proinflammatory cytokine linked to a PD1 ligand. In other aspects, the disclosure provides a chimeric peptide comprising a cytokine peptide and a PD1 ligand peptide.

In certain aspects, the disclosure provides a chimeric peptide comprising a cytokine peptide and an anti-PD1 antibody.

In another different aspect, the disclosure provides a nucleic acid molecule comprising a sequence encoding a chimeric peptide of the disclosure.

In yet another different aspect, the disclosure provides a pharmaceutical composition comprising a chimeric peptide of the disclosure.

In still yet another different aspect, the disclosure provides a method of treating a subject diagnosed with cancer comprising administering to the subject a pharmaceutical composition of the disclosure.

In another aspect is a method to treat a tumor by (1) identifying a subject with a tumor; and (2) administering to the subject a therapeutically effective amount of a combination therapy described herein.

In another aspect is a method for treating a viral infection, by administering to the subject a therapeutically effective amount of a combination therapy described herein.

In some embodiments of the various methods provided herein, a pharmaceutical composition of the disclosure is administered in combination with a PD-1 inhibitor. In certain embodiments, the PD-1 inhibitor is an anti-PD-1 antibody. In some embodiments, the anti-PD-1 antibody is an antagonistic antibody. In some embodiments, the PD-1 inhibitor is selected from the group consisting of nivolumab, pembrolizumab, pidilizumab, REGN2810, PDR 001, and MEDI0680.

In other embodiments, of the various methods provided herein, a pharmaceutical composition of the disclosure is administered in combination with a PD-L1 inhibitor. In certain embodiments, the PD-L1 inhibitor is an anti-PD-L1 antibody. In some embodiments, the anti-PD-L1 antibody is an antagonistic antibody. In some embodiments, the PD-L1 inhibitor is selected from the group consisting of durvalumab, avelumab, atezolizumab, or BMS-936559, STI-A1010, STI-A1011, STI-A1012, STI-A1013, STI-A1014, and STI-A1015.

BRIEF DESCRIPTION OF THE FIGURES

The application file contains at least one drawing executed in color. Copies of this patent application publication with color drawing(s) will be provided by the Office upon request and payment of the necessary fee.

FIG. 1A, FIG. 1B, FIG. 1C, FIG. 1D, FIG. 1E and FIG. 1F depict a diagram, immunoblot and graphs showing the generation and in vitro evaluation of OMCP-mutIL2. (FIG. 1A) Schematic structure of OMCP-mutIL2. (FIG. 1B) Molecular weight of OMCP-mutIL2 compared to mutIL2 and wild-type IL2. IL2, mutIL2, and OMCP-mutIL2 were produced in mammalian cells and have higher molecular weights due to glycosylation. The lower migrating band for mutIL2 corresponds to unglycosylated protein, likely due to lysis of the producing cells. Based on differences in molecular weight all cytokines and construct were administered on a molar basis with 1 μl of 4.4 μM solution defined as 1000 IU equivalents (IUe) herein. This effectively allows for equimolar comparison between IL2, mutIL2 and OMCP-mutIL2 despite different molecular weights. (FIG. 1C, FIG. 1D) In vitro activation of NJ lymphocyte subsets after 36 hours of culture in 100 IUe of cytokines or OMCP-mutIL2 construct. (FIG. 1E, FIG. 1F) Proliferation of B6 lymphocyte subsets after 5-day culture in 1000 IUe/ml of cytokines or OMCP-mutIL2 construct. Graphs representative of 3-6 replicates per condition. black=saline; blue=wtIL2, red=OMCP-mutIL2, green=mutIL2.

FIG. 2A, FIG. 2B, FIG. 2C, FIG. 2D, FIG. 2E, FIG. 2F, FIG. 2G, FIG. 2H, FIG. 2I, FIG. 2J, FIG. 2K, FIG. 2L, FIG. 2M, FIG. 2N and FIG. 2O depict graphs and images showing in vivo dosing of IL2 and IL2 constructs. Animal mortality (FIG. 2A) and morbidity assessed by weight loss (FIG. 2B) accumulation of ascites and pleural fluid (representative syringe-FIG. 2C; average from all mice in the group-FIG. 2D) and (FIG. 2E) organ inflammation after administration of wtIL2. Animal mortality (FIG. 2F, FIG. 2H, FIG. 2J) and morbidity as assessed by weight loss (FIG. 2G, FIG. 2I, FIG. 2K) after administration of high dose wtIL2 (FIG. 2F, FIG. 2G), OMCP-mutIL2 (FIG. 2H, FIG. 2I) and mutIL2 (FIG. 2J, FIG. 2K) in anti-AsialoGM1 (solid line) or rabbit IgG-treated (dotted line) in A/J mice. Weight loss (FIG. 2L), ascites (representative syringe-FIG. 2M; average from all mice in the group-FIG. 2N) and organ inflammation (FIG. 2O) in mice treated with 200,000 IUe of either wt IL2, OMCP-mutIL2 or mutIL2. All graphs represent 46 animals per treatment condition. ns p>0.05; *p<0.05; **p<0.01; ***p<0.001; black=saline; blue=wtIL2, red=OMCP-mutIL2, green=mutIL2.

FIG. 3A, FIG. 3B, FIG. 3C, FIG. 3D, FIG. 3E, FIG. 3F, FIG. 3G, FIG. 3H, FIG. 3I and FIG. 3J depict graphs and images showing immunologic changes associated with IL2 and IL2 construct administration in vivo. (FIG. 3A, FIG. 3B) Total splenocyte counts after a five-day course of 200,000 IUe of IL2 (blue), mutIL2 (green) and OMCP-mutIL2 (red). (FIG. 3C) NK cell expansion and activation after IL2, mutIL2, OMCP-mutIL2, high dose IL2, high dose mutIL2 and IL2/anti-IL2 complexes measured by cell counts in the spleen (top) and KLRG1 upregulation (bottom). (FIG. 3D) CD4⁺Foxp3⁺ T_reg expansion and activation as measured by cell counts in the spleen (top) and ICOS upregulation (bottom) as well as (FIG. 3E) NK/T_reg ratio in the spleen. Expansion of splenocytes (FIG. 3F, FIG. 3G) and NK cells (FIG. 3H) in B6 mice treated with 750,000 IUe of cytokine or construct. T_reg expansion and activation (FIG. 3I) as well as NK:T_reg ratio (FIG. 3J) in the spleen of B6 mice. All graphs represent an average cell count±SEM from 5-10 mice per group. ns p>0.05; *p<0.05; **p<0.01; ***p<0.001; black=saline; blue=wtIL2, red=OMCP-mutIL2, green=mutIL2.

FIG. 4A, FIG. 4B, FIG. 4C, FIG. 4D and FIG. 4E depict graphs and images showing cytokine-mediated tumor immunotherapy. (FIG. 4A) In vivo cytotoxicity for YAC-1 lymphoma after intravenous injection. (FIG. 4B, FIG. 4C) LLC tumor growth after a five-day course of 750,000 IUe of cytokine treatment given as ten doses on days 5-10 post tumor injection. LLC tumor growth in mice depleted on NK cells (FIG. 4D) or mutant mice deficient in NKG2D (FIG. 4E). Data represents 5-6 mice per group. ns p>0.05; *p<0.05; **p<0.01; ***p<0.001; black=saline; blue=wtlL2, red=OMCP-mutIL2, green=mutIL2.

FIG. 5A, FIG. 5B, FIG. 5C, FIG. 5D, FIG. 5E, FIG. 5F, FIG. 5G, FIG. 5H, FIG. 5I, FIG. 5J and FIG. 5K depict graphs and a schematic showing IL2 signaling in NK cells. (FIG. 5A, FIG. 5B) Serum levels after injection of 1×10⁶ IUe of fluorochrome-labeled cytokine or construct i.v. (FIG. 5C) Degranulation of NK cells in the presence of cytokines and pentameric OMCP-mediated crosslinking of NKG2D as measured by surface CD107a expression at 1000 IUe/ml. STAT5 phosphorylation in isolated NK cells from NJ (FIG. 5D) or B6 mice (FIG. 5E) by increasing doses of cytokine. Decay in STAT5 phosphorylation after a 15 minute stimulation by 1000 IUe/ml (FIG. 5F) or 100 IUe/ml (FIG. 5G) of IL2 or OMCP-mutIL2. (FIG. 5H) Proposed model of competition between NK cells and stromal cells for IL2. (FIG. 5I) STAT5 phosphorylation of B6 NK cells in the presence of other splenocytes by wtIL2 and OMCP-mutIL2. (FIG. 5J) STAT5 phosphorylation of wild-type or NKG2D^−/− NK cells by wtIL2 and OMCP-mutIL2 in the presence of competing splenocytes. (FIG. 5K) STAT5 phosphorylation, as measured by fold change over saline-treated controls, of wild-type NK cells in the presence of competing splenocytes treated with saturating concentrations of rat anti-mouse CD25 (clone 3C7) or rat IgG isotype control.

FIG. 6 depicts graphs showing B6 NK cells are preferentially activated by low dose OMCP-mutIL2 but this selectivity disappears at the highest doses of cytokine or in the absence of NKG2D expression by NK cells. Left two graphs show B6 NK cells and right two graphs show BK NKG2D^−/− NK cells.

FIG. 7A, FIG. 7B and FIG. 7C depict imaging showing that inspection of the viscera demonstrates limited food consumption after a 5-day course of 200,000 or 750,000 IUe of wtIL2. FIG. 7D depicts a graph showing that unlike the A/J strain, B6 mice are able to tolerate higher doses of wtIL2 with only moderate weight loss after 750,000 IUe. Higher doses of 1,500,000 IUe IL2 resulted in increased weight loss. Doses above this regimen led to animal death.

FIG. 8A depicts a graph showing that NJ mice treated with IL2/anti-IL2 antibodies or high dose mutIL2 lost significant weight during treatment. The majority of IL2/anti-IL2 treated mice could not survive the full 200,000 IUe dosing and were sacrificed four days after starting treatment thus receiving 160,000-180,000 IUe. FIG. 8B depicts a graph and flow cytometric plot showing NK expansion with ULBP3-mutIL2 and lower doses of OMCP-mutIL2 in NJ spleen (top). NK activation, as measured by surface KLRG1 expression on NK cells treated with 200,000 IUe of mutIL2 (green) or ULBP3-mutIL2 (purple) in NJ spleen (bottom). FIG. 8C and FIG. 8D depict graphs showing that unlike the case for NK cells, little expansion of CD8⁺ or CD4⁺Foxp3⁻ T cells was evident in either IL2, OMCP-mut-IL2, or mutIL2 treated mice. FIG. 8E depicts a graph showing weight loss in B6 mice treated with high dose mutIL2 or IL2/anti-IL2 antibody complex. FIG. 8F and FIG. 8G depict graphs showing expansion of CD8⁺ or CD4⁺Foxp3⁻ T cells in cytokine treated B6 mice. Graphs represent 5-10 mice per group.

FIG. 9A and FIG. 9B depict graphs showing in vitro lysis of NJ tumors, such as LM2 lung adenocarcinoma (FIG. 9A) or YAC-1 lymphoma (FIG. 9B) by bulk splenocytes after a five day course of 200,000 IUe of cytokine given over ten doses. FIG. 9C shows in vitro lysis of LLC lung cancer by B6 splenocytes treated with 750,000 IUe of cytokines or constructs given over five days in ten doses.

FIG. 10A depicts flow cytometric plots showing that plate bound anti-NKG2D antibody (clone A10)-mediated augmentation of NK degranulation with cytokines added at 1000 IUe/ml. FIG. 10B depicts a flow cytometric plot showing CD69 levels on NK cells cultured at 100 IUe/ml of OMCP-mut-IL2 or mutIL2 with pentameric OMCP.

FIG. 11A, FIG. 11B and FIG. 11C depict a schematic of the differential IL2 binding and activation in vivo. (FIG. 11A) Regular wild-type IL2 preferentially binds to cells such as CD4⁺Foxp3⁺ T_regs and vascular endothelium, both of which express the high affinity α chain along with the signaling β and γ chains of the IL2 receptor. (FIG. 11B) The R38A and F42K mutations in IL2 decrease affinity for the α chain of the IL2 receptor. (FIG. 11C) By linking R38A/F42K IL2 to the high affinity NKG2D ligand OMCP delivery and binding of this cytokine to NKG2D-expressing CTLs such as NK cells and activated CD8⁺ T cells is increased. Width of arrows indicates proposed strength of IL2 binding and/or signaling.

FIG. 12 depicts a schematic of the experimental design of immunotherapy experiments.

FIG. 13 depicts a schematic of the experimental design of vaccination experiments.

FIG. 14A and FIG. 14B depict graphs showing lung cancer susceptible and resistant strains of mice. (FIG. 14A) AJ and 129 mouse strains are susceptible to lung cancer as evidenced by tumor burden whereas B6 and C3H mouse strains are resistant to lung cancer as evidenced by tumor burden. (FIG. 14B) Upon incubation with freshly isolated NK cells from the various mouse strains, B6 and C3H NK cells result in significantly more LM2 lung carcinoma cell lysis than AJ and 129 NK cells.

FIG. 15 depicts a graph showing that in human men, a greater percentage of NK cells appear to produce TNFα in “resistant” patients versus “susceptible” patients.

FIG. 16 depicts a graph showing that ex vivo cytokine activation can reverse natural killer cell dysfunction. Mouse NK Cells that did not show significant lysis of cancer cells (NK cells from 129 & AJ strains) were much more effective at lysis when treated with IL2. NK cells from cancer-resistant strains also showed increase % of specific lysis.

FIG. 17A, FIG. 17B, FIG. 17C, FIG. 17D, FIG. 17E and FIG. 17F depict graphs showing binding of fluorescently labeled construct tested in vitro at 37 degrees in bulk splenocytes. The construct appears to only bind to NK cells (express NKG2D). Red line is OMCP-IL2 construct. (FIG. 17A) DX5+CD3− NK cell; (FIG. 17B) CD4+CD3+ T cells; (FIG. 17C) CD8⁺ CD3+ T cells; (FIG. 17D) CD11C+CD11b− DCs; (FIG. 17E) CD11c−CD11b+ Macs; (FIG. 17F) CD19+CD3− B cells.

FIG. 18 depicts a schematic dosing regimen for IL2 or IL2 constructs.

FIG. 19 depicts a schematic dosing regimen for IL2 or IL2 constructs after irradiation.

FIG. 20A, FIG. 20B and FIG. 20C depict images and alignments of the OMCP structure. (FIG. 20A) Ribbon diagram of CPXV OMCP. Secondary structure elements are noted, S for beta strands and H for helix. The α1/α2 portions of the platform domain are indicated in cyan and magenta, respectively. (FIG. 20B) Ribbon diagram of the α1/α2 domain of MICA (PDB identifier 1 HYR), with the α3 domain removed for clarity. Residues that contact NKG2D are colored yellow. (FIG. 20C) Structure alignment of OMCP with NKG2DLs. The mature sequences of OMCP_BR (CPXV-BR-018; GenBank accession number NP_619807; PDB identifier 4FFE) and OMCP_MPX (MPXV-ZAR_1979_005-198; N3R; GenBank accession number AAY97396) are aligned with the ectodomain sequences of MICA (1HYR), MICB (1JE6), ULBP3 (1KCG), and RAE-1β (1JFM). Known NKG2D contact residues for NKG2DLs are indicated in yellow. Asn residues likely to be glycosylated are noted by black boxes in panel C and as black side chains in panels A and B. OMCPbr=SEQ ID NO:13; OMCPmpx=SEQ ID NO:14; MICA=SEQ ID NO:15; MICB=SEQ ID NO:16; ULBP3=SEQ ID NO:17; and RAE-1B=SEQ ID NO:18

FIG. 21 depicts a graph showing OMCP-targeted delivery of IL15. Higher levels of CD25 are evident when IL15 is delivered by OMCP vs naked cytokine alone in equimolar doses.

FIG. 22 depicts a graph showing that the D132R mutation in OMCP significantly decreases its NKG2D binding. NK expansion and activation in the presence of mutIL2, OMCP-mutIL2, and D132ROMCP-mutIL2 was tested. The D132R mutation ameliorated the superiority of natural killer cell activation over cytokine alone.

FIG. 23 depicts various embodiments of the invention. 1. depicts OMCP helix 2 linked to cytokine. 2. depicts pegylation of the composition. 3. depicts a composition comprising engineered glycans. 4. depicts various linker lengths and compositions. 5. depicts an antibody linked to a cytokine. For example a Fab specific NKG2D antibody. 6. depicts a NKG2DL linked to a cytokine. For example, MIC or ULBP. 7 depicts an alternative OMCP linked to a cytokine. For example, OMCP max could represent gain of function for NKG2D binding and mutant OMCP could represent loss of function for NKG2D binding. 8. depicts re-targeting of the OMCP in a composition. For example, the OMCP may be directed to NKG2A, NKG2C, NKG2E, etc. 9. depicts other viral protein liked to a cytokine. For example, the other viral protein may also bind to receptors on immune cells. 10. depicts OMCP linked to mutant cytokines. It is understood that the OMCP sequence could be from various sources such as cowpox or monkeypox. Also, Fc-chimeras of OMCP and IL2, and variants thereof may be used.

FIG. 24A and FIG. 24B depict the structure of OMCP in complex with NKG2D. (FIG. 24A) OMCP bound to NKG2D. OMCP is colored magenta and the protomers of NKG2D are colored cyan (“A”) and yellow (“B”). NKG2D^A makes contacts primarily with the H2a helix and NKG2D^B with H2b. Mutations introduced to facilitate alternate crystal packing are shown in red. The S193-S194 bond is shown as a ball on each NKG2D protomer. The asparagines of putative hNKG2D glycosylation sites are shown in orange. The asparagine of the confirmed N-glycan site of OMCP is shown green (data not shown) (FIG. 24B) View of the interface between OMCP-NKG2D. The α2 domain of OMCP is shown in the front with the α1 domain behind. OMCP and NKG2D are shown with cartoon representations for the main chain, with the side chains of contact residues shown as sticks. Hydrogen bonds and salt bridges are indicated with green dotted lines.

FIG. 25A, FIG. 25B and FIG. 25C depicts the interface of OMCP and NKG2D. (FIG. 25A) The local environment of the OMCP-NKG2D binding interface surrounding the D132R residue. The D132R mutation ablates OMCP-NKG2D binding. (FIG. 25B) A representative experiment for binding of WT and (D132R) OMCP to NKG2D by SPR. 100 nM of OMCP or (D132R) OMCP were injected at 50 μl/min over flowcells containing immobilized biotinylated murine NKG2D. (FIG. 25C) Ba/F3 cells transduced with NKG2D, FCRL5, or empty vector were stained with OMCP tetramers (solid line), D132R tetramers (dashed line), or WNV DIII tetramer control (gray histogram). Representative results from three independent experiments.

FIG. 26A, FIG. 26B, FIG. 26C and FIG. 26D depict the differences in the β5′-β5 loop (L2) of human and murine NKG2D. (FIG. 26A, FIG. 26B) Superimposition of mNKG2D (grey) (PDB ID: 1HQ8) with the structure of OMCP-hNKG2D (yellow and cyan). Core binding residues Y152 (Y168) and Y199 (Y215) are positionally conserved, while core binding residue M184 (1200) is not. (FIG. 26C) Surface representation of OMCP (magenta) interacting with the β5′-β5 loop. (FIG. 26D) Conservation of M184 and Q185. Only the NKG2D of mice, rats, guinea pigs, and flying foxes (not shown) differ. Conservation score is as computed by the ConSurf server. Human, organgutan, chimpanzee, gibbon, macaque-SEQ ID NO:19; Green monkey-SEQ ID NO:20; Marmoset-SEQ ID NO:21; Mouse-SEQ ID NO:22; Rat-SEQ ID NO:23; Guinea pig-SEQ ID NO:24; Ground squirrel-SEQ ID NO:25; Deer mouse-SEQ ID NO:26; Naked mole rat-SEQ ID NO:27; Prairie vole-SEQ ID NO:28; European shrew-SEQ ID NO:29; Star-nosed mole-SEQ ID NO:30; Chinese hamster-SEQ ID NO:31; Cat-SEQ ID NO:32.

FIG. 27A, FIG. 27B, FIG. 27C, FIG. 27D, FIG. 27E, FIG. 27F, FIG. 27G, FIG. 27H and FIG. 27I depict a novel NKG2D binding adaptation and FIG. 27J depicts secondary structure alignment of various NKG2DLs. Surface representation of NKG2D and surface and cartoon representations of OMCP, MICA and ULBP3. Buried surface areas for NKG2D^A and NKG2D^B are indicated in cyan and yellow, respectively. Buried surface area by NKG2D is indicated for OMCP (magenta), MICA (green), and ULBP3 (orange). The core binding residues of NKG2D and NKG2D-binding elements of NKG2DLs are indicated. NKG2D (FIG. 27A) and OMCP (FIG. 27B, FIG. 27C) binding interactions. NKG2D (FIG. 27D) and MICA (FIG. 27E, FIG. 27F) binding interactions. NKG2D (FIG. 27G) and ULBP3 (FIG. 27H, FIG. 27I) binding interactions. (FIG. 27J) Alignment by secondary structure of NKG2DLs (PDB ID: OMCP (4FFE), MICA (1HYR), MICB (1JE6), ULBP3 (1KCG) and RAE-1β (1JSK)). Contact residues are indicated for OMCP (magenta), MICA (green), ULBP3 (orange) and RAE-1β (bold and italics). Secondary structure elements are noted above the sequence (arrow for beta sheets, cylinders for alpha helices). Predicted glycan sites are highlighted in black. OMCPbr=SEQ ID NO:13; OMCPmpx=SEQ ID NO:14; MICA=SEQ ID NO:15; MICB=SEQ ID NO:16; ULBP3=SEQ ID NO:17; and RAE-1B=SEQ ID NO:18

FIG. 28A, FIG. 28B, FIG. 28C, FIG. 28D and FIG. 28E depict activation of NK cells by cell-associated OMCP. Model depicting NKG2D interaction with (FIG. 28A) host, (FIG. 28B) cancer-induced, (FIG. 28C) viral, or (FIG. 28D) chimeric ligands. Binding interactions that lead to NKG2D-mediated signaling are indicated by DAP10 tyrosine phosphorylation (red filled circles). (FIG. 28E) IL2-activated splenocytes were used as cytotoxic effectors against stably transduced Ba/F3 cell lines. Splenocytes were activated with 200 U/ml of IL2 for 24 hours. Labeled target cells were co-incubated with activated splenocytes for 4 hours at effector:target ratios of 10:1, 20:1, and 40:1. Killing was measured by incorporation of 7AAD by CFSE-labeled target cells using flow cytometry. Representative data from five independent experiments is shown

FIG. 29A and FIG. 29B depict the electron density supporting a cis peptide conformation. Stereo view of the β5-β6 loop of hNKG2D. Residues 193-Ala-Ser-Ser-Phe-Lys-197 (SEQ ID NO:33) is displayed for the OMCP-hNKG2D structure (yellow) and the structure of hNKG2D alone (grey). The 2Fo-Fc map for OMCP-hNKG2D is displayed at 2a.

FIG. 30A and FIG. 30B depicts graphs showing survival curves of C57Bl/6J mice following infection with West Nile Virus (WNV). Mice were treated with OMCP-IL2, OMCP(D132R)-IL2, IL2, IL(38R/42A) or PBS after infection with WNV. Infection with OMCP-IL2 and IL2(38R/42A) resulted in survival beyond 21 days in 40% of mice compared to 0 mice following treatment with PBS or OMCP(D132R)-IL2.

FIG. 31A, FIG. 31B, FIG. 31C and FIG. 31D depicts flow cytometry data showing that OMCP-Mutant IL2 activates NK and CD8⁺ T cells. FIG. 31A shows that a relatively higher proportion of NK cells was evident in the OMCP-mutant IL2 group. FIG. 31B shows that perforin levels were higher in OMCP-mutant IL2 treated NK cells (red) compared to saline (black), IL2 (blue) or mutant IL2 (green) treated ones. FIG. 31C shows that similar to NK cells, higher intracellular levels of perforin were evident in CD8⁺ T cells treated with OMCP-mutant IL2 compared to other conditions. FIG. 31D shows that when gating on CD4⁺Foxp3+CD45RA− T cells a relatively higher proportion of activated CD25+CD127− regulatory T cells was evident in IL2 treated peripheral blood lymphocyte cultures compared to other conditions.

FIG. 32 depicts a schematic of the various IL18-OMCP constructs. Three versions were made, each having OMCP attached to either WT human IL-18, WT murine IL-18, or mutant human IL-18 (which inhibits its interaction with IL-18BP).

FIG. 33 depicts a flow cytometry plot showing that IL18-OMCP activates NK cells. Peripheral blood lymphocytes were cultured for 48 hours in 4.4 μM of either wild-type IL18 (blue), OMCP-IL18 (red) or saline (black). Activation of CD56+CD3-Natural killer cells, as measured by surface CD69 expression, was superior by OMCP-IL18 compared to wild-type IL18.

FIG. 34 depicts lungs of mice cohorts treated with isotype antibody, anti-PD-1 antibody, OMCP-IL2 and isotype antibody, and anti-PD-1 antibody and OMCP.

FIG. 35 shows lung weights as measured from the lungs from the mice cohorts of FIG. 34 .

FIG. 36 depicts various embodiments of the invention. 1. A composition is depicted comprising full-length PDL1 or PDL2 linked to a cytokine. 2. A composition is depicted comprising a PDL1 or PDL2 derived peptide linked to a cytokine. 3. A composition is depicted comprising PDL1 or PDL2 linked to a cytokine, wherein the composition is pegylated. 4. A composition is depicted comprising PDL1 or PDL2 linked to a cytokine, wherein the composition comprises N-glycan. 5. A composition is depicted comprising PDL1 or PDL2 linked to a cytokine, wherein the linker comprises various sequences and various lengths. 6. A composition is depicted comprising a Fab specific antibody for PD1 linked to a cytokine. 7. A composition is depicted comprising various PD1 ligands, including mutated versions of PDL1 or PDL2, linked to a cytokine. PDL1 or PDL2 may be mutated to have improved binding affinity or weaker binding affinity. 8 A composition is depicted comprising PDL1 or PDL2 linked to a mutated cytokine. It is understood that the PDL1 and PDL2 sequence could be from various sources such as human, mouse, or monkey. Also, Fc-chimeras of PDL1 or PDL2 and IL2, and variants thereof may be used.

FIG. 37A, FIG. 37B, FIG. 37C, FIG. 37D and FIG. 37E depict graphs showing NK cell physiology after in vitro expansion with either wild-type IL-2 (blue) or OMCP-mutIL-2 (red). FIG. 37A depicts expansion of NK cells. FIG. 37B depicts PD1 expression on NK cells. FIG. 37C depicts NK cell proliferation. FIG. 37C depicts viability of NK cells. FIG. 37E depicts flow cytometry plots of Tim3 and Lag3 expression on NK cells.

FIG. 38A, FIG. 38B, FIG. 38C, FIG. 38D and FIG. 38E depict graphs showing T cell physiology after in vitro expansion with either wild-type IL-2 (blue) or OMCP-mutIL-2 (red). FIG. 38A depicts expansion of T cells. FIG. 38B depicts PD1 expression on T cells. FIG. 38C depicts T cell proliferation. FIG. 38C depicts viability of T cells. FIG. 38E depicts flow cytometry plots of Tim3 and Lag3 expression on T cells.

FIG. 39A, FIG. 39B, FIG. 39C and FIG. 39D depict graphs showing anti-NKG2D antibody-mediated delivery of R38A/F42K mutant IL-2. At 10 U/ml OMCP-mutant IL-2 demonstrated a trend toward increased perforin levels over antibody-mediated delivery but it did not reach statistical significance (FIG. 39A). At 100 U/ml NK cells treated with 2HL2 and 2LH2 antibodies synthesized as much perforin as OMCP-mutIL-2 treated cells but lower levels of perforin were evident in 1HL2 and 1LH2 treated NK cells (FIG. 39B). Higher levels of CD25 were evident in wild-type IL-2 treated cultures over all constructs (FIG. 39C, FIG. 39D). Data representative of 4-7 separate experiments. *=p<0.05 and ns=p>0.05.

DETAILED DESCRIPTION OF THE INVENTION

Certain compositions and methods described herein provide for delivery of cytokines to a defined cell via a NKG2D ligand. The fusion of a cytokine to a NKG2D ligand which specifically binds to the NKG2D receptor on the target cell creates an “address” for delivery of the cytokine. Specifically, using the invention disclosed herein, IL2 is directly targeted to lymphocytes, such as natural killer (NK) cells and CD8+ cytotoxic T lymphocytes (CTLs), via an anti-NKG2D antibody. However other NKG2D ligands, including but not limited to the OMCP ligand, ULBP1, ULBP2, ULBP3, H60, Rae-1α, Rae-1β, Rae-1δ, Rae-1γ, MICA, MICB, h-HLA-A, could also be used instead of an anti-NKG2D antibody. Specific delivery of IL2 to lymphocytes will enhance the efficacy of IL2, which could lead to reduced dosages and a significant decrease in associated toxicity. This methodology may be used for other cytokines, including, but not limited to, IL15, IL18, interferons, and members of the tumor necrosis family including, but not limited to TNF-alpha, OX40L, a 4-1BB ligand, TRAIL, Fas ligand, lymphotoxin-alpha, lymphotoxin-beta, CD30L, CD40L, CD27L and RANKL.

Other compositions and methods described herein provide for the activation and recruitment of NK cells and CTLs to a particular cell or tissue via the combination of a ligand to the NKG2D receptor and a targeting molecule. Specifically, in certain aspects, using the invention disclosed herein, NK cells and CTLs are recruited to a target cell via a composition comprising the OMCP ligand or a portion thereof and a targeting molecule. The targeting molecule permits recruitment of the NK cells and CTLs to the particular target cell wherein the OMCP ligand or a portion thereof provides for recruitment, and in some instance, activation, of the NK cells and CTLs resulting in a site-specific response. Targeting molecules may include any molecule that is capable of binding to a target specific to a cell in a disease state or to the extracellular matrix surrounding the diseased cell including, but not limited to, receptor ligands and antibodies. Specific aspects of the invention are described in detail below.

I. Composition

In an aspect, the invention encompasses a composition comprising a cytokine linked to an immune cell surface protein targeting ligand. In a specific aspect, the cytokine is linked to an NKG2D ligand. In another aspect, the cytokine is linked to a ligand targeting the PD1 surface protein. The composition may further comprise a linker to connect the cytokine to the ligand. The cytokine, ligand and linker are described in greater detail below. It should be understood that any of the cytokines described in detail below can be linked to any of the ligands described in detail below in the absence or presence of any of the linkers described below. In another aspect, the invention provides a nucleic acid molecule encoding a cytokine, a ligand, and optionally a linker.

(a) Cytokine

As used herein, a “cytokine” is a small protein (˜5-20 kDa) that is important in cell signaling. Cytokines are released by cells and affect the behavior of other cells and/or the cells that release the cytokine. Non-limiting examples of cytokines include chemokines, interferons, interleukins, lymphokines, tumor necrosis factor, monokines, and colony stimulating factors. Cytokines may be produced by a broad range of cells including, but not limited to, immune cells such as macrophages, B lymphocytes, T lymphocytes, mast cells and monocytes, endothelial cells, fibroblasts and stromal cells. A cytokine may be produced by more than one type of cell. Cytokines act through receptors and are especially important in the immune system, modulate the balance between humoral and cell-based immune responses, and regulate maturation, growth and responsiveness of cell populations. Cytokines are important in host responses to infection, immune responses, inflammation, trauma, sepsis, cancer and reproduction. A cytokine of the invention may be a naturally occurring cytokine or may be a mutated version of a naturally occurring cytokine. As used herein, “naturally occurring”, which may also be referred to as wild-type, includes allelic variances. A mutated version or “mutant” of a naturally occurring cytokine refers to specific mutations that have been made to the naturally occurring sequence to alter the function, activity and/or specificity of the cytokine. In one embodiment, the mutations may enhance the function, activity and/or specificity of the cytokine. In another embodiment, the mutations may decrease the function, activity and/or specificity of the cytokine. The mutation may include deletions or additions of one or more amino acid residues of the cytokine.

Cytokines may be classified based on structure. For example, cytokines may be classified into four types: the four-α-helix bundle family, the IL1 family, the IL17 family and the cysteine-knot cytokines. Members of the four-α-helix bundle family have three-dimensional structures with four bundles of α-helices. This family is further divided into three sub-families: the IL2 subfamily, the interferon (IFN) subfamily and the IL10 subfamily. The IL2 subfamily is the largest and comprises several non-immunological cytokines including, but not limited to, erythropoietin (EPO) and thrombopoietin (TPO). In certain embodiments, a cytokine of the composition is a cytokine from the four-α-helix bundle family or a mutant thereof. A skilled artisan would be able to determine cytokines within the four-α-helix bundle family. In other embodiments, a cytokine of the composition is an IL2 subfamily cytokine or a mutant thereof. Non-limiting examples of members of the IL2 subfamily include IL2, IL4, IL7, IL9, IL15 and IL21. In a specific embodiment, a cytokine of the composition is IL2 or a mutant thereof. In certain embodiments, a cytokine of the composition is IL15 or a mutant thereof. The sequence information for the full length human IL15 amino acid sequence can be found using, for example, the GenBank accession number CAG46777.1, AAI00962.1 or AAI00963.1. The sequence information for the full length human IL15 mRNA sequence can be found using, for example, the GenBank accession number CR542007.1, KJ891469.1, NM_172175.2, NM_000585.4 or CR541980.1. A skilled artisan will appreciate that IL15 may be found in a variety of species and methods of identifying analogs or homologs of IL15 are known in the art as described in detail below.

In another embodiment, a cytokine of the invention is an IL1 family cytokine or a mutant thereof. The IL1 family is a group of 11 cytokines, which plays a central role in the regulation of immune and inflammatory responses. Generally, the IL1 family of cytokines are proinflammatory cytokines that regulate and initiate inflammatory responses. Non-limiting examples of IL1 family cytokines include IL1α, IL1β, IL1Ra, IL18, IL36Ra, IL36α, IL37, IL36β, IL36γ, IL38, and IL33. IL1 family members have a similar gene structure. A skilled artisan would be able to determine cytokines within the IL1 family. In certain embodiments, a cytokine of the composition is IL18 or a mutant thereof. The sequence information for the full length human IL18 amino acid sequence can be found using, for example, the GenBank accession number CAG46771.1. The sequence information for the full length human IL18 mRNA sequence can be found using, for example, the GenBank accession number KR710147.1, CR542001.1, CR541973.1 or KJ897054.1. A skilled artisan will appreciate that IL18 may be found in a variety of species and methods of identifying analogs or homologs of IL18 are known in the art as described in detail below.

In other embodiments, a cytokine of the composition is an interferon subfamily cytokine or a mutant thereof. Interferons are named for their ability to “interfere” with viral replication by protecting cells from virus infection. IFNs also have other functions: they activate immune cells, such as natural killer cells and macrophages; they increase host defenses by up-regulating antigen presentation by virtue of increasing the expression of major histocompatibility complex (MHC) antigens. Based on the type of receptor through which they signal, human interferons have been classified into three major types: Type I IFN, Type II IFN, and Type III IFN. Type I IFNs bind to a specific cell surface receptor complex known as the IFN-α/β receptor (IFNAR) that consists of IFNAR1 and IFNAR2 chains. Non-limiting examples of type I interferons present in humans are IFN-α, IFN-β, IFN-ε, IFN-κ and IFN-ω. Thus, in certain embodiments, a cytokine of the composition is a Type 1 IFN cytokine or a mutant thereof, including, but not limited to wild-type and mutant forms of IFN-α, IFN-β, IFN-ε, IFN-κ and IFN-ω. Type II IFNs bind to IFNGR that consists of IFNGR1 and IFNGR2 chains. Non-limiting examples of type II interferons present in humans is IFN-γ. Thus, in certain embodiments, a cytokine of the composition is a Type II IFN cytokine or a mutant thereof, including, but not limited to wild-type and mutant forms of IFN-γ. Type III IFNs signal through a receptor complex consisting of IL10R2 (also called CRF2-4) and IFNLR1 (also called CRF2-12). Non-limiting examples of type III interferons include IFN-λ1, IFN-λ2 and IFN-λ3 (also called IL29, IL28A and IL28B respectively). Thus, in certain embodiments, a cytokine of the composition is a Type III IFN cytokine or a mutant thereof, including, but not limited to wild-type and mutant forms of IFN-λ1, IFN-λ2 and IFN-λ3.

In other embodiments, a cytokine of the composition is a member of the tumor necrosis factor superfamily (TNFSF), or a mutant thereof. TNFSF members are pro-inflammatory cytokines mainly expressed by immune cells which induce an inflammatory state and stimulate immune cell function. At least 18 TNFSF homologues exist, including but not limited to, TNF (TNFalpha), CD40L (TNFSF5), CD70 (TNFSF7; CD27L), EDA, FASL (TNFSF6; Fas ligand), LTA (TNFSF1; lymphotoxin-alpha), LTB (TNFSF3; lymphotoxin-beta), TNFSF4 (OX40L), TNFSF8 (CD153), TNFSF9 (4-1BBL), TNFSF10 (TRAIL), TNFSF11 (RANKL; receptor activator of nuclear factor kappa-B ligand), TNFSF12 (TWEAK), TNFSF13, TNFSF13B, TNFSF14, TNFSF15, TNFSF18. Thus, in certain embodiments, a cytokine of the composition is a member of the tumor necrosis factor superfamily or a mutant thereof, including, but not limited to TNF (TNFalpha), CD40L (TNFSF5), CD70 (TNFSF7; CD27L), EDA, FASL (TNFSF6), LTA (TNFSF1), LTB (TNFSF3), TNFSF4 (OX40L), TNFSF8 (CD153), TNFSF9 (4-1BBL), TNFSF10 (TRAIL), TNFSF11 (RANKL), TNFSF12 (TWEAK), TNFSF13, TNFSF13B, TNFSF14, TNFSF15, TNFSF18.

In certain embodiments, a cytokine of the composition is OX40L, a fragment thereof, or a mutant thereof. The sequence information for the full length human OX40L amino acid sequence can be found using, for example, the GenBank accession number XP_016857719.1, XP_016857718.1, XP_016857717.1, XP_011508266.2, NP_001284491.1, NP_003317.1, CAG46830.1. The sequence information for the full length human OX40L mRNA sequence can be found using, for example, the GenBank accession number XR_001737396.1, XR_001737395.1, XR_001737394.1, XR_001737393.1, XM_017002230.1, XM_017002229.1, XM_017002228.1, XM_011509964.2, NM_001297562.1, NM_003326.4. A skilled artisan will appreciate that OX40L may be found in a variety of species and methods of identifying analogs or homologs of OX40L are known in the art as described in detail below.

A skilled artisan will appreciate that OX40L may be found in a variety of species. Non-limiting examples include mouse (NP_033478.1), pig (NP_001020388.1), cattle (NP_001192644.1), rat (NP_446004.1), rabbit (NP_001075454.1), goat (XP_013825644.1), sheep (XP_012042680.1), chicken (XP_430147.2), hamster (XP_007610839.1), and dog (XP_003639215.1). It is appreciated that the present invention is directed to analogs of OX40L in other organisms and is not limited to the human analog. Homologs can be found in other species by methods known in the art. For example, sequence similarity may be determined by conventional algorithms, which typically allow introduction of a small number of gaps in order to achieve the best fit. In particular, “percent identity” of two polypeptides or two nucleic acid sequences is determined using the algorithm of Karlin and Altschul (Proc. Natl. Acad. Sci. USA 87:2264-2268, 1993). Such an algorithm is incorporated into the BLASTN and BLASTX programs of Altschul et al. (J. Mol. Biol. 215:403-410, 1990). BLAST nucleotide searches may be performed with the BLASTN program to obtain nucleotide sequences homologous to a nucleic acid molecule of the invention. Equally, BLAST protein searches may be performed with the BLASTX program to obtain amino acid sequences that are homologous to a polypeptide of the invention. To obtain gapped alignments for comparison purposes, Gapped BLAST is utilized as described in Altschul et al. (Nucleic Acids Res. 25:3389-3402, 1997). When utilizing BLAST and Gapped BLAST programs, the default parameters of the respective programs (e.g., BLASTX and BLASTN) are employed. See www.ncbi.nlm.nih.gov for more details. Generally, a homolog will have a least 80, 81, 82, 83, 84, 85, 86, 87, 88, or 89% homology. In another embodiment, the sequence may be at least 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, or 100% homologous to OX40L.

In a specific embodiment, a cytokine of the composition is a wildtype sequence of OX40L. In a specific embodiment, the cytokine may contain the wild-type OX40L fragments such as the sequence set forth in

SEQ ID NO: 57

(QVSHRYPRIQSIKVQFTEYKKEKGFILTSQKEDEIMKVQNNSVIINCDG

FYLISLKGYFSQEVNISLHYQKDEEPLFQLKKVRSVNSLMVASLTYKDKV

YLNVTTDNTSLDDFHVNGGELILIHQNPGEFCVL).

In certain embodiments, these fragments may be connected into a continuous peptide via linker fragments. In a specific embodiment, a cytokine may be the OX40L fragments connected via linker peptides such as the sequence set forth in

SEQ ID NO: 58

(QVSHRYPRIQSIKVQFTEYKKEKGFILTSQKEDEIMKVQNNSVIINCD

GFYLISLKGYFSQEVNISLHYQKDEEPLFQLKKVRSVNSLMVASLTYKD

KVYLNVTTDNTSLDDFHVNGGELILIHQNPGEFCVLGGSGGGSGGGSGQ

VSHRYPRIQSIKVQFTEYKKEKGFILTSQKEDEIMKVQNNSVIINCDGF

YLISLKGYFSQEVNISLHYQKDEEPLFQLKKVRSVNSLMVASLTYKDKV

YLNVTTDNTSLDDFHVNGGELILIHQNPGEFCVLGGSGGGSGGGSGQVS

HRYPRIQSIKVQFTEYKKEKGFILTSQKEDEIMKVQNNSVIINCDGFYL

ISLKGYFSQEVNISLHYQKDEEPLFQLKKVRSVNSLMVASLTYKDKVYL

NVTTDNTSLDDFHVNGGELILIHQNPGEFCVL).

In an alternate embodiment, a cytokine of the composition is a mutated sequence of OX40L. In an embodiment, a mutation is a mutation that causes OX40L to bind to but inhibit signaling of the tumor necrosis factor receptor superfamily, member 4 (TNFRSF4, also known as OX40, also known as CD134). For example, a mutation may be one or more mutations selected from the group of N166A and F180A relative to the full length OX40L sequence in SEQ ID NO:56. In a specific embodiment, a mutated version of OX40L comprises at least one mutation selected from the group consisting of N166A and F180A relative to the full length OX40L sequence in SEQ ID NO:56. In a specific embodiment, a cytokine may contain the mutated OX40L fragments such as the sequence set forth in

SEQ ID NO: 59

(QVSHRYPRIQSIKVQFTEYKKEKGFILTSQKEDEIMKVQNNSVIINCDG

FYLISLKGYFSQEVNISLHYQKDEEPLFQLKKVRSVNSLMVASLTYKDKV

YLNVTTDNTSLDDFHVAGGELILIHQNPGEACVL).

In certain embodiments, these fragments may be connected into a continuous peptide via linker fragments. In a specific embodiment, a cyotokine may be mutated and unmutated OX40L fragments connected via linker peptides such as the sequence set forth in

SEQ ID NO: 60

(QVSHRYPRIQSIKVQFTEYKKEKGFILTSQKEDEIMKVQNNSVIINCDG

FYLISLKGYFSQEVNISLHYQKDEEPLFQLKKVRSVNSLMVASLTYKDKV

YLNVTTDNTSLDDFHVAGGELILIHQNPGEACVLGGSGGGSGGGSGQVSH

RYPRIQSIKVQFTEYKKEKGFILTSQKEDEIMKVQNNSVIINCDGFYLIS

LKGYFSQEVNISLHYQKDEEPLFQLKKVRSVNSLMVASLTYKDKVYLNVT

TDNTSLDDFHVAGGELILIHQNPGEACVLGGSGGGSGGGSGQVSHRYPRI

QSIKVQFTEYKKEKGFILTSQKEDEIMKVQNNSVIINCDGFYLISLKGYF

SQEVNISLHYQKDEEPLFQLKKVRSVNSLMVASLTYKDKVYLNVTTDNTS

LDDFHVNGGELILIHQNPGEFCVL).

In another specific embodiment, a cyotokine may be mutated and unmutated OX40L fragments connected via linker peptides such as the sequence set forth in

SEQ ID NO: 61

(QVSHRYPRIQSIKVQFTEYKKEKGFILTSQKEDEIMKVQNNSVIINCDG

FYLISLKGYFSQEVNISLHYQKDEEPLFQLKKVRSVNSLMVASLTYKDKV

YLNVTTDNTSLDDFHVAGGELILIHQNPGEACVLGGSGGGSGGGSGQVSH

RYPRIQSIKVQFTEYKKEKGFILTSQKEDEIMKVQNNSVIINCDGFYLIS

LKGYFSQEVNISLHYQKDEEPLFQLKKVRSVNSLMVASLTYKDKVYLNVT

TDNTSLDDFHVNGGELILIHQNPGEFCVLGGSGGGSGGGSGQVSHRYPRI

QSIKVQFTEYKKEKGFILTSQKEDEIMKVQNNSVIINCDGFYLISLKGYF

SQEVNISLHYQKDEEPLFQLKKVRSVNSLMVASLTYKDKVYLNVTTDNTS

LDDFHVNGGELILIHQNPGEFCVL).

In certain embodiments, a cytokine of the composition is 4-1BBL, a fragment thereof, or a mutant thereof. The sequence information for the full length human 4-1BBL amino acid sequence can be found using, for example, the GenBank accession number NP_003802.1. The sequence information for the full length human 4-1BBL mRNA sequence can be found using, for example, the GenBank accession number NM_003811.3. A skilled artisan will appreciate that 4-1BBL may be found in a variety of species and methods of identifying analogs or homologs of 4-1BBL are known in the art as described in detail below.

A skilled artisan will appreciate that 4-1BBL may be found in a variety of species. Non-limiting examples include mouse (NP_033430.1), pig (XP_003480863.1), cattle (NP_001306831.1), rat (NP_852049.1), rabbit (XP_008251123.1), goat (XP_013820683.1), sheep (XP_014951136.1), hamster (XP_007627369.1), and dog (XP_005633029.1). It is appreciated that the present invention is directed to analogs of 4-1BBL in other organisms and is not limited to the human analog. Homologs can be found in other species by methods known in the art. For example, sequence similarity may be determined by conventional algorithms, which typically allow introduction of a small number of gaps in order to achieve the best fit. In particular, “percent identity” of two polypeptides or two nucleic acid sequences is determined using the algorithm of Karlin and Altschul (Proc. Natl. Acad. Sci. USA 87:2264-2268, 1993). Such an algorithm is incorporated into the BLASTN and BLASTX programs of Altschul et al. (J. Mol. Biol. 215:403-410, 1990). BLAST nucleotide searches may be performed with the BLASTN program to obtain nucleotide sequences homologous to a nucleic acid molecule of the invention. Equally, BLAST protein searches may be performed with the BLASTX program to obtain amino acid sequences that are homologous to a polypeptide of the invention. To obtain gapped alignments for comparison purposes, Gapped BLAST is utilized as described in Altschul et al. (Nucleic Acids Res. 25:3389-3402, 1997). When utilizing BLAST and Gapped BLAST programs, the default parameters of the respective programs (e.g., BLASTX and BLASTN) are employed. See www.ncbi.nlm.nih.gov for more details. Generally, a homolog will have a least 80, 81, 82, 83, 84, 85, 86, 87, 88, or 89% homology. In another embodiment, the sequence may be at least 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, or 100% homologous to 4-1BBL.

In a specific embodiment, a cytokine of the composition is a wildtype sequence of 4-1BBL. In a specific embodiment, the cytokine may contain the wild-type 4-1BBL fragments such as the sequence set forth in

SEQ ID NO: 65

(ACPWAVSGARASPGSAASPRLREGPELSPDDPAGLLDLRQGMFAQLVAQ

NVLLIDGPLSWYSDPGLAGVSLTGGLSYKEDTKELVVAKAGVYYVFFQLE

LRRVVAGEGSGSVSLALHLQPLRSAAGAAALALTVDLPPASSEARNSAFG

FQGRLLHLSAGQRLGVHLHTEARARHAWQLTQGATVLGLFRVTPEIPAGL

PSPRSE).

In certain embodiments, these fragments may be connected into a continuous peptide via linker fragments. In a specific embodiment, a cytokine may be the 4-1BBL fragments connected via linker peptides such as the sequence set forth in

SEQ ID NO: 66

(ACPWAVSGARASPGSAASPRLREGPELSPDDPAGLLDLRQGMFAQLVAQ

NVLLIDGPLSWYSDPGLAGVSLTGGLSYKEDTKELVVAKAGVYYVFFQLE

LRRVVAGEGSGSVSLALHLQPLRSAAGAAALALTVDLPPASSEARNSAFG

FQGRLLHLSAGQRLGVHLHTEARARHAWQLTQGATVLGLFRVTPEIPAGL

PSPRSEGGSGGGSGGGSGACPWAVSGARASPGSAASPRLREGPELSPDDP

AGLLDLRQGMFAQLVAQNVLLIDGPLSWYSDPGLAGVSLTGGLSYKEDTK

ELVVAKAGVYYVFFQLELRRVVAGEGSGSVSLALHLQPLRSAAGAAALAL

TVDLPPASSEARNSAFGFQGRLLHLSAGQRLGVHLHTEARARHAWQLTQG

ATVLGLFRVTPEIPAGLPSPRSEGGSGGGSGGGSGACPWAVSGARASPGS

AASPRLREGPELSPDDPAGLLDLRQGMFAQLVAQNVLLIDGPLSWYSDPG

LAGVSLTGGLSYKEDTKELVVAKAGVYYVFFQLELRRVVAGEGSGSVSLA

LHLQPLRSAAGAAALALTVDLPPASSEARNSAFGFQGRLLHLSAGQRLGV

HLHTEARARHAWQLTQGATVLGLFRVTPEIPAGLPSPRSE).

In an alternate embodiment, a cytokine of the composition is a mutated sequence of 4-1BBL. In an embodiment, a mutation is a mutation that affects the binding affinity between 4-1BBL and its receptor the tumor necrosis factor receptor superfamily, member 9 (TNFRSF9, also known as 4-1BB, also known as CD137).

In certain embodiments, a cytokine of the invention is an interleukin or mutant thereof. The majority of interleukins are synthesized by helper CD4 T lymphocytes, as well as through monocytes, macrophages, and endothelial cells. Interleukins may promote the development and differentiation of T and B lymphocytes and hematopoietic cells. Non-limiting examples of interleukins include IL1, IL2, IL3, IL4, IL5, IL6, IL7, IL8 (CXCL8), IL9, IL10, IL11, IL12, IL13, IL14, IL15, IL16, IL17, IL18, IL19, IL20, IL21, IL22, IL23, IL24, IL25, IL26, IL27, IL28, IL29, IL30, IL31, IL32, IL33, IL35, or IL36. Thus, in certain embodiments, a cytokine of the composition is an interleukin or a mutant thereof, including, but not limited to wild-type and mutant forms of IL1, IL2, IL3, IL4, IL5, IL6, IL7, IL8 (CXCL8), IL9, IL10, IL11, IL12, IL13, IL14, IL15, IL16, IL17, IL18, IL19, IL20, IL21, IL22, IL23, IL24, IL25, IL26, IL27, IL28, IL29, IL30, IL31, IL32, IL33, IL35, or IL36. In a specific embodiment, a cytokine of the composition is IL2 or a mutant thereof. IL2 is a lymphokine that induces the proliferation of responsive T cells. In addition, it acts on some B cells, via receptor-specific binding, as a growth factor and antibody production stimulant. The IL2 protein is secreted as a single glycosylated polypeptide, and cleavage of a signal sequence is required for its activity. The structure of IL2 comprises a bundle of 4 helices (termed A-D), flanked by 2 shorter helices and several poorly defined loops. Residues in helix A, and in the loop region between helices A and B, are important for receptor binding. Secondary structure analysis suggests similarity to IL4 and granulocyte-macrophage colony stimulating factor (GMCSF). In a specific embodiment, a cytokine of the composition is IL2 or a variant thereof. A variant may be a truncated or mutated IL2. The sequence information for the full length human IL2 amino acid sequence can be found using, for example, the GenBank accession number AAA59140.1 or AAH70338.1. The sequence information for the full length human IL2 mRNA sequence can be found using, for example, the GenBank accession number BC070338.1 or M22005.1.

A skilled artisan will appreciate that IL2 may be found in a variety of species. Non-limiting examples include mouse (AAI16874.1), pig (NP_999026.1), cattle (AAQ10670.1), rat (EDM01295.1), rabbit (AAC23838.1), goat (AAQ10671.1), sheep (ABK41601.1), chicken (AAV35056.1), hamster (ERE88380.1), and dog (AAA68969.1). It is appreciated that the present invention is directed to analogs of IL2 in other organisms and is not limited to the human analog. Homologs can be found in other species by methods known in the art. For example, sequence similarity may be determined by conventional algorithms, which typically allow introduction of a small number of gaps in order to achieve the best fit. In particular, “percent identity” of two polypeptides or two nucleic acid sequences is determined using the algorithm of Karlin and Altschul (Proc. Natl. Acad. Sci. USA 87:2264-2268, 1993). Such an algorithm is incorporated into the BLASTN and BLASTX programs of Altschul et al. (J. Mol. Biol. 215:403-410, 1990). BLAST nucleotide searches may be performed with the BLASTN program to obtain nucleotide sequences homologous to a nucleic acid molecule of the invention. Equally, BLAST protein searches may be performed with the BLASTX program to obtain amino acid sequences that are homologous to a polypeptide of the invention. To obtain gapped alignments for comparison purposes, Gapped BLAST is utilized as described in Altschul et al. (Nucleic Acids Res. 25:3389-3402, 1997). When utilizing BLAST and Gapped BLAST programs, the default parameters of the respective programs (e.g., BLASTX and BLASTN) are employed. See www.ncbi.nlm.nih.gov for more details. Generally a homolog will have a least 80, 81, 82, 83, 84, 85, 86, 87, 88, or 89% homology. In another embodiment, the sequence may be at least 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, or 100% homologous to IL2.

In a specific embodiment, a cytokine of the composition is a wildtype sequence of IL2 such as the sequence set forth in

SEQ ID NO: 5

(APTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKK

ATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGS

ETTFMCEYADETATIVEFLNRWITFCQSIISTLT).

In an alternative embodiment, a cytokine is a mutated version of IL2. In an embodiment, a mutation is a mutation that causes IL2 to preferentially bind the receptor IL2βγ. In another embodiment, a mutation is a mutation that alters the function of IL2 such that IL2 has a decreased affinity for the IL2 receptor alpha (IL2Rα). For example, a mutation may be one or more mutations selected from the group consisting of R38A, F42K and/or C125S relative to SEQ ID NO:5. The C125S mutation may be included to reduce protein aggregation. In a specific embodiment, a mutated version of IL2 comprises at least one mutation selected from the group consisting of R38A, F42K and C125S relative to SEQ ID NO:5. In another specific embodiment, a mutated version of IL2 comprises the mutations R38A, F42K and C125S relative to SEQ ID NO:5. In a specific embodiment, a cytokine of the composition is a mutated sequence of IL2 such as the sequence set forth in

SEQ ID NO: 6

(APTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTAMLTKKFYMPKK

ATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGS

ETTFMCEYADETATIVEFLNRWITFSQSIISTLT).

In an alternative aspect, a toxin is substituted for a cytokine. The term “toxin” means the toxic material or product of plants, animals, microorganisms (including, but not limited to, bacteria, viruses, fungi, rickettsiae or protozoa), or infectious substances, or a recombinant or synthesized molecule, whatever their origin and method of production. A toxin may be a small molecule, peptide, or protein that is capable of causing disease on contact with or absorption by body tissues interacting with biological macromolecules such as enzymes or cellular receptors. A toxin may be a “biotoxin” which is used to explicitly identify the toxin as from biological origin. Biotoxins may be further classified into fungal biotoxins, or short mycotoxins, microbial biotoxins, plant biotoxins, short phytotoxins and animal biotoxins. Non-limiting examples of biotoxins include: cyanotoxins, produced by cyanobacteria, such as microcystins, nodularins, anatoxin-a, cylindrospermopsins, lyngbyatoxin-a, saxitoxin, lipopolysaccharides, aplysiatoxins, BMAA; dinotoxins, produced by dinoflagellates, such as saxitoxins and gonyautoxins; necrotoxins produced by, for example, the brown recluse or “fiddle back” spider, most rattlesnakes and vipers, the puff adder, Streptococcus pyogenes; neurotoxins, produced by, for example, the black widow spider, most scorpions, the box jellyfish, elapid snakes, the cone snail, the Blue-ringed octopus, venomous fish, frogs, palythoa coral, various different types of algae, cyanobacteria and dinoflagellates, such as botulinum toxin (e.g. Botox), tetanus toxin, tetrodotoxin, chlorotoxin, conotoxin, anatoxin-a, bungarotoxin, caramboxin, curare; myotoxins, found in, for example, snake and lizard venoms; and cytotoxins such as ricin, from castor beans, apitoxin, from honey bees, and T-2 mycotoxin, from certain toxic mushrooms. In certain embodiments, a toxin is a cytotoxin. In an embodiment, a cytotoxin is selected from the group consisting of ricin, apitoxin, and T-2 mycotoxin. In a specific embodiment, a toxin is ricin.

In certain embodiments, a cytokine or toxin of the invention may be PEGylated for improved systemic half-life and reduced dosage frequency. In an embodiment, PEG may be added to a cytokine or toxin. As such, a composition of the invention may comprise a cytokine or toxin comprising PEG. In an embodiment, PEG may be selected from the group consisting of PEG-10K, PEG-20K and PEG-40K. Methods of conjugating PEG to a protein are standard in the art. For example, see Kolate et al, Journal of Controlled Release 2014; 192(28): 67-81, which is hereby incorporated by reference in its entirety. Still further, a cytokine or toxin of the invention may be modified to remove T cell epitopes. T cell epitopes can be the cause of an immunogenicity issue upon administration of a composition to a subject. Through their presentation to T cells, they activate the process of anti-drug antibody development. Preclinical screening for T cell epitopes may be performed in silico, followed by in vitro and in vivo validation. T cell epitope-mapping tools such as EpiMatrix can be highly accurate predictors of immune response. Deliberate removal of T cell epitopes may reduce immunogenicity. Other means of improving the safety and efficacy of a composition of the invention by reducing their immunogenicity include humanization and PEGylation.

(b) Ligand

As used herein, a “ligand” is a protein that specifically binds to a receptor on a target cell and is not the corresponding binding partner to the cytokine linked to the ligand. A ligand may be from a eukaryote, a prokaryote or a virus. In certain embodiments, a ligand may be from a virus. The phrase “specifically binds” herein means ligands bind to the target protein with an affinity (K_d) in the range of at least 0.1 mM to 1 pM, or in the range of at least 0.1 pM to 200 nM, or in the range of at least 0.1 pM to 10 nM. A dissociation constant (K_d) measures the propensity of a larger object to separate (dissociate) reversibly into smaller components. The dissociation constant is the inverse of the association constant. The dissociation constant may be used to describe the affinity between a ligand (L) and a target protein (P). As such, K_d=([P]×[L])/[C], wherein C is a ligand-target protein complex and wherein [P], [L] and [C] represent molar concentrations of the protein, ligand and complex, respectively. Methods of determining whether a ligand binds to a target protein are known in the art. For instance, see the Rossi and Taylor, Nature Protocols 2011; 6: 365-387.

A ligand may trigger a signal through its binding to a receptor on a target cell. A receptor is a protein molecule that may be embedded within the plasma membrane surface of a cell that receives chemical signals from outside the cell. When such chemical signals bind to a receptor, they cause some form of cellular/tissue response. In preferred embodiments, a target cell is an immune cell. Accordingly, a ligand of the composition binds to a receptor expressed on immune cells. Non-limiting example of immune cells include macrophages, B lymphocytes, T lymphocytes, mast cells, monocytes, dendritic cells, eosinophils, natural killer cells, basophils, neutrophils. Thus, in certain embodiments, immune cells include, but are not limited to, macrophages, B lymphocytes, T lymphocytes, mast cells, monocytes, dendritic cells, eosinophils, natural killer cells, basophils, neutrophils. In a specific embodiment, an immune cell is a natural killer cell or a T lymphocyte. Non-limiting examples of receptors expressed on immune cells include major histocompatibility complex (MHC; e.g. MHCI, MHCII, and MHCIII), toll-like receptors (TLRs; e.g. TLR1, TLR2, TLR3, TLR4, TLR5, TLR6, TLR7, TLR8, TLR9, TLR10, TLR11, TLR12, and TLR13), CD94/NKG2 family receptor, endothelin receptors, signaling lymphocytic activation molecule (SLAM) family of receptors. Thus, in certain embodiments, a receptor on a target cell includes, but is not limited to, major histocompatibility complex (MHC; e.g. MHCI, MHCII, and MHCIII), toll-like receptors (TLRs; e.g. TLR1, TLR2, TLR3, TLR4, TLR5, TLR6, TLR7, TLR8, TLR9, TLR10, TLR11, TLR12, and TLR13), CD94/NKG2 family receptor, endothelin receptors, signaling lymphocytic activation molecule (SLAM) family of receptors. In a specific embodiment, the receptor on a target cell is a CD94/NKG2 family receptor. In another specific embodiment, a ligand of the composition specifically binds to a receptor expressed on natural killer (NK) cells and CD8⁺ cytotoxic T lymphocytes (CTLs). In preferred embodiments, a ligand of the composition does not specifically bind to a receptor on vascular endothelial cells or regulatory T cells (T_regs).

A receptor expressed on NK cells and CTLs may be a CD94/NKG2 family receptor or KLRG1. KLRG1 (Killer cell lectin-like receptor subfamily G member 1) is a protein that in humans is encoded by the KLRG1 gene. CD94/NKG2 family receptors are a family of C-type lectin receptors which are expressed predominantly on the surface of NK cells and a subset of CD8+ T-lymphocyte. These receptors stimulate or inhibit cytotoxic activity of NK cells, therefore they are divided into activating and inhibitory receptors according to their function. CD94/NKG2 recognize MHC class I-related glycoproteins. CD94/NKG2 family includes seven members: NKG2A, NKG2B, NKG2C, NKG2D, NKG2E, NKG2F and NKG2H. Thus, in certain embodiments, a ligand of the invention specifically binds to a receptor selected from the group consisting of NKG2A, NKG2B, NKG2C, NKG2D, NKG2E, NKG2F and NKG2H. NKG2 receptors are transmembrane proteins type II which dimerize with CD94 molecule. CD94 contains a short cytoplasmic domain and it is responsible for signal transduction. Therefore NKG2 receptors form disulfide bonded heterodimers. NKG2D represents an exception, it is a homodimer. NKG2A and NKG2B receptors transmit inhibitory signal. NKG2C, NKG2E and NKG2H are activating receptors. NKG2D is activating receptor as well but it couples with adaptor protein DAP10 which carries signaling motif YINM (SEQ ID NO:34). Src or Jak kinases phosphorylate DAP10, which can then associate with p85 subunit of PI(3)K or adaptor molecule Grb2. This signaling triggers actin reorganization (cell polarization) and degranulation. NKG2F receptor function has not been clarified yet.

In a specific embodiment, a ligand of the composition specifically binds to the NKG2D receptor. NKG2D is an activating receptor found on NK cells and CD8⁺ T cells (both αβ and γδ). The structure of NKG2D consists of two disulphide-linked type II transmembrane proteins with short intracellular domains incapable of transducing signals. The function of NKG2D on CD8⁺ T cells is to send co-stimulatory signals to activate them. In an embodiment, a ligand that binds to NKG2D may be an anti-NKG2D antibody. An “anti-NKG2D” includes all antibodies that specifically bind an epitope within NKG2D. The term “antibody” includes the term “monoclonal antibody”. “Monoclonal antibody” refers to an antibody that is derived from a single copy or clone, including e.g., any eukaryotic, prokaryotic, or phage clone. Monoclonal antibodies can be produced using e.g., hybridoma techniques well known in the art, as well as recombinant technologies, phage display technologies, synthetic technologies or combinations of such technologies and other technologies readily known in the art. Further by “antibody” is meant a functional monoclonal antibody, or an immunologically effective fragment thereof; such as an Fab, Fab′, or F(ab′)2 fragment thereof. As long as the protein retains the ability specifically to bind its intended target, it is included within the term “antibody.” Also included within the definition “antibody” for example are single chain forms, generally designated Fv, regions, of antibodies with this specificity. These scFvs are comprised of the heavy and light chain variable regions connected by a linker. Methods of making and using scFvs are known in the art. Additionally, included within the definition “antibody” are single-domain antibodies, generally designated sdAb, which is an antibody fragment consisting of a single monomeric variable antibody domain. A sdAb antibody may be derived from camelids (VHH fragments) or cartilaginous fishes (V_NAR fragments). As used herein “humanized antibody” includes an anti-NKG2D antibody that is composed partially or fully of amino acid sequence sequences derived from a human antibody germ line by altering the sequence of an antibody having non-human complementarity determining regions (“CDR”). The simplest such alteration may consist simply of substituting the constant region of a human antibody for the murine constant region, thus resulting in a human/murine chimera which may have sufficiently low immunogenicity to be acceptable for pharmaceutical use. Preferably, however, the variable region of the antibody and even the CDR is also humanized by techniques that are by now well known in the art. The framework regions of the variable regions are substituted by the corresponding human framework regions leaving the non-human CDR substantially intact, or even replacing the CDR with sequences derived from a human genome. CDRs may also be randomly mutated such that binding activity and affinity for NKG2D is maintained or enhanced in the context of fully human germ line framework regions or framework regions that are substantially human. In certain embodiments, an anti-NKG2D antibody is a Fab, Fab′, or F(ab′)2 fragment.

In one particular embodiment, the anti-NKG2D antibody is KYK-1 or KYK-2 as described in Kwong, et al, J Mol Biol. 2008 Dec. 31; 384(5):1143-56. The light chain of KYK-1 comprises the amino acid sequence set forth in

SEQ ID NO: 35

(QPVLTQPSSVSVAPGETARIPCGGDDIETKSVHWYQQKPGQAPVLVIYD

DDDRPSGIPERFFGSNSGNTATLSISRVEAGDEADYYCQVWDDNNDEWVF

GGGTQLTVL)

and the heavy chain of the KYK-1 comprises the amino acid sequence set forth in

SEQ ID NO: 36

(EVQLVESGGGVVQPGGSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVA

FIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAKD

RFGYYLDYWGQGTLVTVSS).

The light chain of KYK-2 comprises the amino acid sequence set forth in

SEQ ID NO: 37

(QSALTQPASVSGSPGQSITISCSGSSSNIGNNAVNWYQQLPGKAPKLLI

YYDDLLPSGVSDRFSGSKSGTSAFLAISGLQSEDEADYYCAAWDDSLNGP

VFGGGTKLTVL)

and

the heavy chain of the KYK-2 comprises the amino acid sequence set forth in

SEQ ID NO: 38

(QVQLVESGGGLVKPGGSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVA

FIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAKD

RGLGDGTYFDYWGQGTTVTVSS).

In another particular embodiment, the anti-NKG2D antibody is an scFv derived from KYK-1. For example, the KYK-1 scFv comprises the amino acid sequence set forth in

SEQ ID NO: 39

(QPVLTQPSSVSVAPGETARIPCGGDDIETKSVHWYQQKPGQAPVLVIYD

DDDRPSGIPERFFGSNSGNTATLSISRVEAGDEADYYCQVWDDNNDEWVF

GGGTQLTVLGGGGSGGGGSGGGGSGGGGSEVQLVESGGGVVQPGGSLRLS

CAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTIS

RDNSKNTLYLQMNSLRAEDTAVYYCAKDRFGYYLDYWGQGTLVTVSS).

Alternatively, the KYK-1 scFv comprises the amino acid sequence set forth in

SEQ ID NO: 40

(EVQLVESGGGVVQPGGSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVA

FIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAKD

RFGYYLDYWGQGTLVTVSSGGGGSGGGGSGGGGSGGGGSQPVLTQPSSVS

VAPGETARIPCGGDDIETKSVHWYQQKPGQAPVLVIYDDDDRPSGIPERF

FGSNSGNTATLSISRVEAGDEADYYCQVWDDNNDEWVFGGGTQLTVL).

In another particular embodiment, the anti-NKG2D antibody is an scFv derived from KYK-2. For example, the KYK-2 scFv comprises the amino acid sequence set forth in

SEQ ID NO: 41

(QSALTQPASVSGSPGQSITISCSGSSSNIGNNAVNWYQQLPGKAPKLLI

YYDDLLPSGVSDRFSGSKSGTSAFLAISGLQSEDEADYYCAAWDDSLNGP

VFGGGTKLTVLGGGGSGGGGSGGGGSGGGGSQVQLVESGGGLVKPGGSLR

LSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYDGSNKYYADSVKGRFT

ISRDNSKNTLYLQMNSLRAEDTAVYYCAKDRGLGDGTYFDYWGQGTTVTV

SS).

Alternatively, the KYK-2 scFv comprises the amino acid sequence set forth in

SEQ ID NO: 42

(QVQLVESGGGLVKPGGSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVA

FIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAKD

RGLGDGTYFDYWGQGTTVTV).

As stated above, the various KYK-1 and KYK-2 antibodies or scFv thereof may be combined with any of the cytokines disclosed herein, in the absence or presence of any of the linkers described herein to provide the compositions or chimeric peptides of the present invention. It should also be understood that the KYK-1 and KYK-2 antibodies are examples of antibodies suitable for use in the present compositions and one of skill in the art, based on this disclosure, will understand that other anti-NKG2D antibodies will be suitable as well.

In another embodiment, ligands that bind to NKG2D share an MHC class I-related α1α2 superdomain that constitutes the common site for interaction with NKG2D. Non-limiting examples of ligands that bind to NKG2D include MHC class I-related glycoproteins such as MIC family proteins (i.e., MICA, MICB), UL16-binding family proteins (i.e., ULBP1, ULBP2, ULPB3, ULBP4, ULBP5, ULBP6), retinoid acid early induce gene 1 (Rae1)-like proteins (i.e., Rae1α, Rae1β, Rae1γ, Rae1δ, Rae1ε), members of the H60 protein family (i.e., H60a, H60b, H60c), h-HLA-A, as well as Multi in mice and OMCP. In certain embodiments, a ligand is a MHC class-I-related glycoprotein. In other embodiments, a ligand of the invention is selected from the group consisting of MICA, MICB, ULBP1, ULBP2, ULBP3, ULBP4, ULBP5, ULBP6, Rae1α, Rae1β, Rae1γ, Rae1δ, Rae1ε, H60a, H60b, H60c, h-HLA-A, Multi and OMCP. In an embodiment, a ligand is a UL16-binding family protein or a MIC family protein. In a specific embodiment, a ligand is selected from the group consisting of ULBP1, ULBP2, ULBP3, ULBP4, ULBP5, and ULBP6. In another specific embodiment, a ligand is ULBP3. In a specific embodiment, a ligand is OMCP or a variant thereof. A variant may be a truncated or mutated OMCP that has about the same binding affinity of the full length OMCP. In an embodiment, a variant may be a truncated or mutated OMCP that has a slightly lower binding affinity relative to the binding affinity of the full length OMCP. In another embodiment, a variant is a truncated or mutated OMCP that has a slightly higher binding affinity relative to the binding affinity of the full length OMCP. Methods to determine binding affinity of a ligand to target protein are known in the art and described above. OMCP specifically binds to NKG2D with a binding affinity of about 0.1 to about 5 nM. For example, OMCP specially binds to human NKG2D with a binding affinity of about 0.2 nM and mouse NKG2D with a binding affinity of about 3 nM. In a preferred embodiment, OMCP or a variant thereof binds to human NKG2D with a binding affinity of about 1000 nM to about 0.1 nM. In certain embodiments, OMCP or a variant thereof binds to human NKG2D with a binding affinity of about 100 nM to about 0.1 nM, about 10 nM to about 0.1 nM, or about 1 nM to about 0.1 nM. In other embodiments, OMCP or a variant thereof binds to human NKG2D with a binding affinity of about 1000 nM to about 1 nM, or about 1000 nM to about 10 nM, or about 1000 nM to about 100 nM. In still other embodiments, OMCP or a variant thereof binds to human NKG2D with a binding affinity of about 100 nM to about 1 nM, or about 100 nM to 10 nM. For example, OMCP or a variant thereof binds to human NKG2D with a binding affinity of about 1000 nM, about 500 nM, about 100 nM, about 50 nM, about 10 nM, about 9 nM, about 8 nM, about 7 nM, about 6 nM about 5 nM, about 4 nM, about 3 nM, about 2 nM, about 1 nM, about 0.9 nM, about 0.8 nM, about 0.7 nM, about 0.6 nM, about 0.5 nM, about 0.4 nM, about 0.3 nM, about 0.2 nM or about 0.1 nM. In another embodiment, a variant is a truncated or mutated OMCP that has binding affinity for one or more NKG2 family receptors other than NKG2D. For example, a variant is a truncated or mutated OMCP that has binding affinity for one or more NKG2 family receptors selected from the group consisting of NKG2A, NKG2B, NKG2C, NKG2E, NKG2F and NKG2H. Mutations to OMCP may be rationally selected via structure-based knowledge or mutations to OMCP may be identified via selection-based mutagenesis. In certain embodiments, mutations may be rationally selected to occur in the OMCP-NKG2D interface to either enhance or reduce binding affinity. Amino acids involved in binding at the OMCP-NKG2D interface are described in the Examples.

The structure of OMCP consists of an MHCI-like α1/α2 platform domain (FIG. 20A). The platform domain of OMCP has been trimmed to have only a six-stranded beta sheet with shorter flanking helices. The helix of the OMCP α1 domain (H1) is continuous, while the helix of the α2 domain is broken into two regions (H2a and H2b). The helices flank a six-stranded beta sheet and together form the characteristic platform that defines MHC proteins. Like other NKG2DLs (FIG. 20B), the alpha helices of OMCP are close together and thus have no groove for binding peptides or other ligands like antigen-presenting MHC platform domains. OMCP contains one disulfide bond between S5 and H2b, and this disulfide bond is conserved in most NKG2DLs (FIG. 20C). In certain embodiments, a ligand of the invention comprises one or more of the α helices of a MHC class I-related glycoprotein. In other embodiments, a ligand of the invention consists of one or more of the α helices of a MHC class I-related glycoprotein. More specifically, a ligand of the invention comprises the α1 domain (H1), α2 domain (H2), H2a, H2b, or combinations thereof of a MHC class I-related glycoprotein. Or, a ligand of the invention consists of the α1 domain (H1), α2 domain (H2), H2a, H2b, or combinations thereof of a MHC class I-related glycoprotein. In a specific embodiment, a ligand of the invention comprises the α2 domain (H2) of a MHC class I-related glycoprotein. In another specific embodiment, a ligand of the invention consists of the α2 domain (H2) of a MHC class I-related glycoprotein. A skilled artisan would be able to determine the location of the α helices in other MHC class I-related glycoproteins, for example, using sequence alignment (see FIG. 20C, which is reproduced from Lazear et al. J Virol 2013; 87(2): 840-850, which is hereby incorporated by reference in its entirety). In an embodiment, a ligand of the invention comprises one or more of the α helices of OMCP. In another embodiment, a ligand of the invention comprises the α1 domain (H1), α2 domain (H2), H2a, H2b, or combinations thereof of OMCP. In still another embodiment, a ligand of the invention comprises the α2 domain (H2) of OMCP. In a specific embodiment, a ligand of the invention consists of one or more of the α helices of OMCP. In another specific embodiment, a ligand of the invention consists of the α1 domain (H1), α2 domain (H2), H2a, H2b, or combinations thereof of OMCP. In still another specific embodiment, a ligand of the invention consists of the α2 domain (H2) of OMCP.

The sequence information for the full length OMCP amino acid sequence can be found using, for example, the GenBank accession number 4FFE_Z, 4FFE_Y or 4FFE_X. A skilled artisan will appreciate that homologs of OMCP may be found in other species or viruses. For example, see Lefkowitz et al, Nucleic Acids Res 2005; 33: D311-316, which is herein incorporated by reference in its entirety, which describes eighteen OMCP variants between cowpox and monkeypox virus strains. In an embodiment, OMCP is from an orthopoxvirus. In a specific embodiment, OMCP is from a cowpox virus or a monkeypox virus. In another specific embodiment, OMCP is from the Brighton Red strain of cowpoxvirus. Homologs can be found in other species by methods known in the art. For example, sequence similarity may be determined by conventional algorithms, which typically allow introduction of a small number of gaps in order to achieve the best fit. In particular, “percent identity” of two polypeptides or two nucleic acid sequences is determined using the algorithm of Karlin and Altschul (Proc. Natl. Acad. Sci. USA 87:2264-2268, 1993). Such an algorithm is incorporated into the BLASTN and BLASTX programs of Altschul et al. (J. Mol. Biol. 215:403-410, 1990). BLAST nucleotide searches may be performed with the BLASTN program to obtain nucleotide sequences homologous to a nucleic acid molecule of the invention. Equally, BLAST protein searches may be performed with the BLASTX program to obtain amino acid sequences that are homologous to a polypeptide of the invention. To obtain gapped alignments for comparison purposes, Gapped BLAST is utilized as described in Altschul et al. (Nucleic Acids Res. 25:3389-3402, 1997). When utilizing BLAST and Gapped BLAST programs, the default parameters of the respective programs (e.g., BLASTX and BLASTN) are employed. See www.ncbi.nlm.nih.gov for more details. Generally a homolog will have a least 80, 81, 82, 83, 84, 85, 86, 87, 88, or 89% homology. In another embodiment, the sequence may be at least 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, or 100% homologous to OMCP.

A skilled artisan will appreciate that structural homologs of OMCP may be found in other species or viruses. A structural homolog may be a protein that is structurally related but the sequence is a distal homolog. For example, OMCP has low sequence identity for endogenous NKG2D however it was discovered that OMCP would bind to NKG2D based on structural homology. Structural homologs can be found in other species by methods known in the art. For example, protein structure prediction may be determined by various databases, such as Phyre and Phyre2. Such databases generate reliable protein models that may be used to determine structural homologs. The main results table in Phyre2 provides confidence estimates, images and links to the three-dimensional predicted models and information derived from either Structural Classification of Proteins database (SCOP) or the Protein Data Bank (PDB) depending on the source of the detected template. For each match a link takes the user to a detailed view of the alignment between the user sequence and the sequence of known three-dimensional structure. See www.sbg.bio.ic.ac.uk/phyre2/ for more details. Generally, a structural homolog will have a least 50, 51, 52, 53, 54, 55, 56, 57, 58, or 59% confidence with OMCP. In an embodiment, a structural homolog will have a least 60, 61, 62, 63, 64, 65, 66, 67, 68, or 69% confidence with OMCP. In another embodiment, a structural homolog will have a least 70, 71, 72, 73, 74, 75, 76, 77, 78, or 79% confidence with OMCP. In still another embodiment, a structural homolog will have a least 80, 81, 82, 83, 64, 85, 86, 87, 88, or 89% confidence with OMCP. In still yet another embodiment, a structural homolog may have at least 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, or 100% confidence with OMCP. The structural information for OMCP-human NKG2D may be found using the PDB ID: 4PDC.

In a specific embodiment, a ligand of the composition is a sequence of OMCP such as the sequence set forth in

SEQ ID NO: 7

(HKLAFNFNLEINGSDTHSTVDVYLDDSQIITFDGKDIRPTIPFMIGDEI

FLPFYKNVFSEFFSLFRRVPTSTPYEDLTYFYECDYTDNKSTFDQFYLYN

GEEYTVKTQEATNKNMWLTTSEFRLKKWFDGEDCIMHLRSLVRKMEDSKR

NTG).

In an embodiment, a ligand of the composition is a sequence of OMCP comprising at least 80% identity to SEQ ID NO:7. For example, the ligand may have about 80%, about 81%, about 82%, about 83%, about 84%, about 85%, about 86%, about 87%, about 88%, about 89%, about 90%, about 91%, about 92%, about 93%, about 94%, about 95%, about 96%, about 97%, about 98%, about 99%, or about 100% identity to SEQ ID NO:7.

In another specific embodiment, a ligand of the composition is a sequence of OMCP such as the sequence set forth in

SEQ ID NO: 13

(GHKLAFNFNLEINGSDTHSTVDVYLDDSQIITFDGKDIRPTIPFMIGDE

IFLPFYKNVFSEFFSLFRRVPTSTPYEDLTYFYECDYTDNKSTFDQFYLY

NGEEYTVKTQEATNKNMWLTTSEFRLKKWFDGEDCIMHLRSLVRKMEDSK

R).

In an embodiment, a ligand of the composition is a sequence of OMCP comprising at least 80% identity to SEQ ID NO:13. For example, the ligand may have about 80%, about 81%, about 82%, about 83%, about 84%, about 85%, about 86%, about 87%, about 88%, about 89%, about 90%, about 91%, about 92%, about 93%, about 94%, about 95%, about 96%, about 97%, about 98%, about 99%, or about 100% identity to SEQ ID NO:13.

In still another specific embodiment, a ligand of the composition is a sequence of OMCP such as the sequence set forth in

SEQ ID NO: 14

(HKLVHYFNLKINGSDITNTADILLDNYPIMTFDGKDIYPSIAFMVGNKL

FLDLYKNIFVEFFRLFRVSVSSQYEELEYYYSCDYTNNRPTIKQHYFYNG

EEYTEIDRSKKATNKNSWLITSGFRLQKWFDSEDCIIYLRSLVRRMEDSN

K).

In an embodiment, a ligand of the composition is a sequence of OMCP comprising at least 80% identity to SEQ ID NO:14. For example, the ligand may have about 80%, about 81%, about 82%, about 83%, about 84%, about 85%, about 86%, about 87%, about 88%, about 89%, about 90%, about 91%, about 92%, about 93%, about 94%, about 95%, about 96%, about 97%, about 98%, about 99%, or about 100% identity to SEQ ID NO:14.

In an alternative aspect, a receptor expressed on immune cells may be PD1. PD1, also known as programmed cell death protein 1 and CD279 (cluster of differentiation 279), is a protein that in humans is encoded by the PDCD1 gene. PD1 is a cell surface receptor that belongs to the immunoglobulin superfamily and is expressed on T cells and pro-B cells. PD1 binds two ligands, PDL1 and PDL2. PD1, functioning as an immune checkpoint, plays an important role in down regulating the immune system by preventing the activation of T-cells. In certain embodiments, a ligand of the composition specifically binds to PD1. In an embodiment, a ligand that specifically binds to PD1 may be an anti-PD1 antibody. An “anti-PD1” includes all antibodies that specifically bind an epitope within PD1. The term “antibody” is described above. In another embodiment, a ligand that specifically binds to PD1 may be PDL1 or PDL2. PDL1 (programmed death-ligand 1 also known as cluster of differentiation 274 (CD274)) or B7 homolog 1 (B7-H1), is a protein that in humans is encoded by the CD274 gene. PDL1 binds to its receptor, PD1, found on activated T cells, B cells, and myeloid cells, to modulate activation or inhibition. The affinity between PDL1 and PD1, as defined by the dissociation constant K_d, is 770 nM. PDL2 (programmed death ligand 2 also known as cluster of differentiation 273 (CD273) or B7DC) is a protein that in humans is encoded by the PDCD1LG2 gene. PDL2 also binds to the PD1 receptor. The affinity between PDL2 and PD1, as defined by the dissociation constant K_d, is 590 nM

The sequence information for full length PDL1 mRNA can be found, for example, using the NCBI accession number NM_014143, NM_001267706, NR 052005, NM_001314029, and the full length amino acid sequence can be found using, for example, the NCBI accession number NP_001300958, NP_001254635, NP 054862. A skilled artisan will appreciate that homologs of PDL1 may be found in other species. In a particular embodiment, PDL1 is derived from Homo sapiens. Sequence similarity may be determined via conventional algorithms, such as described herein above for OMCP. Specifically, “percent identity” of two polypeptides or two nucleic acid sequences Is determined using the BLASTN, BLASTX, and Gapped BLAST programs using the default parameters. See www.ncbi.nlm.nih.gov for more details. Generally, a homolog will have a least 80, 81, 82, 83, 84, 85, 86, 87, 88, or 89% homology. In another embodiment, the sequence may be at least 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, or 100% homologous to PDL1.

In a specific embodiment, a ligand of the composition is a sequence of PDL1 such as the sequence set forth in

SEQ ID NO: 51

(MRIFAVFIFMTYWHLLNAFTVTVPKDLYVVEYGSNMTIECKFPVEKQLD

LAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNAAL

QITDVKLQDAGVYRCMISYGGADYKRITVKVNAPYNKINQRILVVDPVTS

EHELTCQAEGYPKAEVIWTSSDHQVLSGKTTTTNSKREEKLFNVTSTLRI

NTTTNEIFYCTFRRLDPEENHTAELVIPGNILNVSIKICLTLSPST).

In an embodiment, a ligand of the composition is a sequence of PDL1 comprising at least 80% identity to SEQ ID NO:51. For example, the ligand may have about 80%, about 81%, about 82%, about 83%, about 84%, about 85%, about 86%, about 87%, about 88%, about 89%, about 90%, about 91%, about 92%, about 93%, about 94%, about 95%, about 96%, about 97%, about 98%, about 99%, or about 100% identity to SEQ ID NO:51.

In still another specific embodiment, a ligand of the composition is a sequence of PDL1 such as the sequence set forth in

SEQ ID NO: 52

(MRIFAVFIFMTYWHLLNAPYNKINQRILVVDPVTSEHELTCQAEGYPKA

EVIWTSSDHQVLSGKTTTTNSKREEKLFNVTSTLRINTTTNEIFYCTFRR

LDPEENHTAELVIPELPLAHPPNERTHLVILGAILLCLGVALTFIFRLRK

GRMMDVKKCGIQDTNSKKQSDTHLEET).

In an embodiment, a ligand of the composition is a sequence of PDL1 comprising at least 80% identity to SEQ ID NO:52. For example, the ligand may have about 80%, about 81%, about 82%, about 83%, about 84%, about 85%, about 86%, about 87%, about 88%, about 89%, about 90%, about 91%, about 92%, about 93%, about 94%, about 95%, about 96%, about 97%, about 98%, about 99%, or about 100% identity to SEQ ID NO:52.

In still another specific embodiment, a ligand of the composition is a sequence of PDL1 such as the sequence set forth in

SEQ ID NO: 53

(MRIFAVFIFMTYWHLLNAFTVTVPKDLYVVEYGSNMTIECKFPVEKQLD

LAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNAAL

QITDVKLQDAGVYRCMISYGGADYKRITVKVNAPYNKINQRILVVDPVTS

EHELTCQAEGYPKAEVIWTSSDHQVLSGKTTTTNSKREEKLFNVTSTLRI

NTTTNEIFYCTFRRLDPEENHTAELVIPELPLAHPPNERTHLVILGAILL

CLGVALTFIFRLRKGRMMDVKKCGIQDTNSKKQSDTHLEET).

In an embodiment, a ligand of the composition is a sequence of PDL1 comprising at least 80% identity to SEQ ID NO:53. For example, the ligand may have about 80%, about 81%, about 82%, about 83%, about 84%, about 85%, about 86%, about 87%, about 88%, about 89%, about 90%, about 91%, about 92%, about 93%, about 94%, about 95%, about 96%, about 97%, about 98%, about 99%, or about 100% identity to SEQ ID NO:53.

The sequence information for full length PDL2 mRNA can be found for example, using the NCBI accession number NM_025239 and XM_005251600, and the full length amino acid sequence can be found using, for example, the NCBI accession number NP_079515 and XP_005251657. A skilled artisan will appreciate that homologs of PDL1 may be found in other species. In a particular embodiment, PDL2 is derived from Homo sapiens. Sequence similarity may be determined via conventional algorithms, such as described herein above for OMCP. Specifically, “percent identity” of two polypeptides or two nucleic acid sequences Is determined using the BLASTN, BLASTX, and Gapped BLAST programs using the default parameters. See www.ncbi.nlm.nih.gov for more details. Generally, a homolog will have a least 80, 81, 82, 83, 84, 85, 86, 87, 88, or 89% homology. In another embodiment, the sequence may be at least 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, or 100% homologous to PDL2.

In a specific embodiment, a ligand of the composition is a sequence of PDL2 such as the sequence set forth in

SEQ ID NO: 54

(IFLLLMLSLELQLHQIAALFTVTVPKELYIIEHGSNVTLECNFDTGSHV

NLGAITASLQKVENDTSPHRERATLLEEQLPLGKASFHIPQVQVRDEGQY

QCIIIYGVAWDYKYLTLKVKASYRKINTHILKVPETDEVELTCQATGYPL

AEVSWPNVSVPANTSHSRTPEGLYQVTSVLRLKPPPGRNFSCVFWNTHVR

ELTLASIDLQSQMEPRTHPTWLLHIFIPFCIIAFIFIATVIALRKQLCQK

LYSSKDTTKRPVTTTKREVNSAI).

In an embodiment, a ligand of the composition is a sequence of PDL2 comprising at least 80% identity to SEQ ID NO:54. For example, the ligand may have about 80%, about 81%, about 82%, about 83%, about 84%, about 85%, about 86%, about 87%, about 88%, about 89%, about 90%, about 91%, about 92%, about 93%, about 94%, about 95%, about 96%, about 97%, about 98%, about 99%, or about 100% identity to SEQ ID NO:54.

In another specific embodiment, a ligand of the composition is a sequence of PDL2 such as the sequence set forth in

SEQ ID NO: 54

(MIFLLLMLSLELQLHQIAALFTVTVPKELYIIEHGSNVTLECNFDTGSH

VNLGAITASLQKVENDTSPHRERATLLEEQLPLGKASFHIPQVQVRDEGQ

YQCIIIYGVAWDYKYLTLKVKASYRKINTHILKVPETDEVELTCQATGYP

LAEVSWPNVSVPANTSHSRTPEGLYQVTSVLRLKPPPGRNFSCVFWNTHV

RELTLASIDLQSQMEPRTHPTWLLHIFIPFCIIAFIFIATVIALRKQLCQ

KLYSSKDTTKRPVTTTKREVNSAVNLNLWSWEPG).

In an embodiment, a ligand of the composition is a sequence of PDL2 comprising at least 80% identity to SEQ ID NO:54. For example, the ligand may have about 80%, about 81%, about 82%, about 83%, about 84%, about 85%, about 86%, about 87%, about 88%, about 89%, about 90%, about 91%, about 92%, about 93%, about 94%, about 95%, about 96%, about 97%, about 98%, about 99%, or about 100% identity to SEQ ID NO:54.

In another aspect, a ligand of the composition may be Glucocorticoid-induced TNFR-related (GITR) ligand (GITRL). GITR activation by GITRL influences the activity of effector and regulatory T cells, thus participating in the development of immune response against tumors and infectious agents, as well as in autoimmune and inflammatory diseases. GITR triggering stimulates T effector activity and inhibits Treg activity. GITR inhibition may ameliorate autoimmune/inflammatory diseases whereas GITR activation may treat viral, bacterial and parasitic infections, as well as boost immune responses against tumors. GITRL is a type II transmembrane protein expressed at high levels on antigen presenting cells (APC) and endothelial cells.

In certain embodiments, a ligand of the invention is modified for improved systemic half-life and reduced dosage frequency. In an embodiment, N-glycans may be added to a ligand. While the biological function is typically determined by the protein component, carbohydrate can play a role in molecular stability, solubility, in vivo activity, serum half-life, and immunogenicity. The sialic acid component of carbohydrate in particular, can extend the serum half-life of protein therapeutics. Accordingly, new N-linked glycosylation consensus sequences may be introduced into desirable positions in the peptide backbone to generate proteins with increased sialic acid containing carbohydrate, thereby increasing in vivo activity due to a longer serum half-life. In another embodiment, PEG may be added to a ligand. Methods of conjugating PEG to a protein are standard in the art. For example, see Kolate et al, Journal of Controlled Release 2014; 192(28): 67-81, which is hereby incorporated by reference in its entirety. In an embodiment, a composition of the invention may comprise a ligand comprising PEG and/or one or more N-glycans. In an embodiment, PEG is selected from the group consisting of PEG-10K, PEG-20K and PEG-40K. Still further, a ligand of the invention may be modified to remove T cell epitopes. T cell epitopes can be the cause of an immunogenicity issue upon administration of a composition to a subject. Through their presentation to T cells, they activate the process of anti-drug antibody development. Preclinical screening for T cell epitopes may be performed in silico, followed by in vitro and in vivo validation. T cell epitope-mapping tools such as EpiMatrix can be highly accurate predictors of immune response. Deliberate removal of T cell epitopes may reduce immunogenicity. Other means of improving the safety and efficacy of a composition of the invention by reducing their immunogenicity include humanization and PEGylation.

(c) Linker

In an aspect, a composition of the invention further comprises a linker. The linker may be used to connect the cytokine to the ligand. It is to be understood that linking the cytokine to the ligand will not adversely affect the function of the cytokine or the ligand. Suitable linkers include amino acid chains and alkyl chains functionalized with reactive groups for coupling to both the cytokine and the ligand or combinations thereof.

In an embodiment, the linker may include amino acid side chains, referred to as a peptide linker. Amino acid residue linkers are usually at least one residue and can be 50 or more residues, but alone do not specifically bind to the target protein. In an embodiment, a linker may be about 1 to about 10 amino acids. In another embodiment, a linker may be about 10 to about 20 amino acids. In still another embodiment, a linker may be about 20 to about 30 amino acids. In still yet another embodiment, a linker may be about 30 to about 40 amino acids. In different embodiments, a linker may be about 40 to about 50 amino acids. In other embodiments, a linker may be more than 50 amino acids. For instance, a linker may be 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49 or 50 amino acids. In a specific embodiment, a linker is about 20 to about 30 amino acids. In another specific embodiment, a linker is about 26 amino acids.

Any amino acid residue may be used for the linker provided the linker does not specifically bind to the target protein. Typical amino acid residues used for linking are glycine, serine, alanine, leucine, tyrosine, cysteine, lysine, glutamic and aspartic acid, or the like. For example, a linker may be (AAS)_n, (AAAL)_n (SEQ ID NO:68), (G_nS)_n or (G₂S)_n, wherein A is alanine, S is serine, L is leucine, and G is glycine and wherein n is an integer from 1-20, or 1-10, or 3-10. Accordingly, n may be 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19 or 20. Thus, in certain embodiments, a linker includes, but is not limited to, (AAS)_n, (AAAL)_n (SEQ ID NO:68), (G_nS)_n or (G₂S)_n, wherein A is alanine, S is serine, L is leucine, and G is glycine and wherein n is an integer from 1-20, or 1-10, or 3-10. A linker may comprise one or more epitope tags. For instance, a linker may comprise 1, 2, 3, 4, 5, 6, 7 or 8 epitope tags. In a specific embodiment, a linker comprises 2 epitope tags. Non-limiting examples of epitope tags include FLAG tag (DYKDDDK epitope (SEQ ID NO:9)), HA tag (YPYDVPDYA epitope (SEQ ID NO:10)), His tag (6×-His or 8×-His), Myc tag (EQKLISEEDL epitope (SEQ ID NO:11)) and V5 tag (GKPIPNPLLGLDST epitope (SEQ ID NO:12)). In an embodiment, a linker may comprise at least one tag selected from the group consisting of a FLAG tag and a His tag. In a specific embodiment, a linker comprises a FLAG tag and a His tag. In another specific embodiment, a linker comprises the sequence set forth in SEQ ID NO:8 (GSSGSSDYKDDDDKHHHHHHHHGSSGSS).

In another embodiment, an alkyl chain linking group may be coupled to the cytokine by reacting the terminal amino group or the terminal carboxyl group with a functional group on the alkyl chain, such as a carboxyl group or an activated ester. Subsequently the ligand is attached to the alkyl chain to complete the formation of the complex by reacting a second functional group on the alkyl chain with an appropriate group on the ligand. The second functional group on the alkyl chain is selected from substituents that are reactive with a functional group on the ligand while not being reactive with the cytokine. For example, when the ligand incorporates a functional group, such as a carboxyl group or an activated ester, the second functional group of the alkyl chain linking group can be an amino group or vice versa. It will be appreciated that formation of the conjugate may require protection and deprotection of the functional groups present in order to avoid formation of undesired products. Protection and deprotection are accomplished using protecting groups, reagents, and protocols common in the art of organic synthesis. Particularly, protection and deprotection techniques employed in solid phase peptide synthesis may be used. It will be appreciated that linking groups may alternatively be coupled first to the ligand and then to the cytokine.

An alternative chemical linking group to an alkyl chain is polyethylene glycol (PEG), which is functionalized in the same manner as the alkyl chain described above. Such a linker may be referred to as a heterobifunctional PEG linker or a homobifunctional PEG linker. Non-limiting examples of heterobifunctional PEG linkers include: O-(2-Aminoethyl)-O′-[2-(biotinylamino)ethyl]octaethylene glycol; O-(2-Aminoethyl)-O′-(2-carboxyethyl)polyethylene glycol hydrochloride M_p 3000; O-(2-Aminoethyl)-O′-(2-carboxyethyl)polyethylene glycol 5,000 hydrochloride M_p 5,000; O-(2-Aminoethyl)polyethylene glycol 3,000 Mp 3,000; O-(2-Aminoethyl)-O′-(2-(succinylamino)ethyl)polyethylene glycol hydrochloride Mp 10,000; O-(2-Azidoethyl)heptaethylene glycol; O-[2-(Biotinylamino)ethyl]-O′-(2-carboxyethyl)undecaethylene glycol; 21-[D(+)-Biotinylamino]-4,7,10,13,16,19-hexaoxaheneicosanoic acid; O-(2-Carboxyethyl)-O′-[2-(Fmoc-amino)-ethyl]heptacosaethylene glycol; O-(2-Carboxyethyl)-O′-(2-mercaptoethyl)heptaethylene glycol; O-(3-Carboxypropyl)-O′-[2-(3-mercaptopropionylamino)ethyl]-polyethylene glycol M_w 3000; O-(3-Carboxypropyl)-O′-[2-(3-mercaptopropionylamino)ethyl]-polyethylene glycol M_w 5000; O—[N-(3-Maleimidopropionyl)aminoethyl]-O′-[3-(N-succinimidyloxy)-3-oxopropyl]heptacosaethylene glycol; and O-[2-(3-Tritylthiopropionylamino)ethyl]polyethylene glycol M_p 3,000. Non-limiting examples of homobifunctional PEG linkers include: MAL-PEG-MAL (Bifunctional Maleimide PEG Maleimide); OPSS-PEG-OPSS (OPSS: orthopyridyl disulfide; PDP-PEG-PDP); HS-PEG-SH (Bifunctional Thiol PEG Thiol); SG-PEG-SG (Bifunctional PEG Succinimidyl Glutarate NHS ester); SS-PEG-SS (Bifunctional PEG Succinimidyl Succinate NHS ester); GAS-PEG-GAS (Bifunctional PEG Succinimidyl ester NHS-PEG-NHS); SAS-PEG-SAS (Bifunctional PEG Succinimidyl ester NHS-PEG-NHS); Amine-PEG-Amine (Bifunctional PEG Amine NH2-PEG-NH2); AC-PEG-AC (Bifunctional Acrylate PEG Acrylate); ACA-PEG-ACA (Bifunctional Polymerizable PEG Acrylate Acrylamide); Epoxide-PEG-Epoxide (Bifunctional PEG Epoxide or EP); NPC-PEG-NPC (Bifunctional NPC PEG, Nitrophenyl Carbonate); Aldehyde-PEG-Aldehyde (ALD-PEG-ALD, bifunctional PEG propionaldehyde); AA-PEG-AA (Acid-PEG-Acid, AA—acetic acid or carboxyl methyl); GA-PEG-GA (Acid-PEG-Acid, GA: Glutaric acid); SA-PEG-SA (Bifunctional PEG carboxylic acid-Succinic Acid); GAA-PEG-GAA (Bifunctional PEG carboxylic acid, Glutaramide Acid); SAA-PEG-SAA (Bifunctional PEG carboxylic acid, Succinamide Acid); Azide-PEG-Azide (Bifunctional PEG azide, N3-PEG-N3); Alkyne-PEG-Alkyne (Bifunctional alkyne or acetylene PEG); Biotin-PEG-Biotin (Bifunctional biotin PEG linker); Silane-PEG-Silane (Bifunctional silane PEG); Hydrazide-PEG-Hydrazide (Bifunctional PEG Hydrazide); Tosylate-PEG-Tosylate (Bifunctional PEG Tosyl); and Chloride-PEG-Chloride (Bifunctional PEG Halide).

In certain embodiments, a linker of the invention may be modified for improved systemic half-life and reduced dosage frequency. In an embodiment, N-glycans are added to a linker. While the biological function is typically determined by the protein component, carbohydrates can play a role in molecular stability, solubility, in vivo activity, serum half-life, and immunogenicity. The sialic acid component of carbohydrate in particular, can extend the serum half-life of protein therapeutics. Accordingly, new N-linked glycosylation consensus sequences may be introduced into desirable positions in the peptide backbone to generate proteins with increased sialic acid containing carbohydrate, thereby increasing in vivo activity due to a longer serum half-life. In another embodiment, PEG is added to a linker. Methods of conjugating PEG to a protein are standard in the art. For example, see Kolate et al, Journal of Controlled Release 2014; 192(28): 67-81, which is hereby incorporated by reference in its entirety. In an embodiment, a composition of the invention comprises a ligand comprising PEG and/or one or more N-glycans. In an embodiment, PEG is selected from the group consisting of PEG-10K, PEG-20K and PEG-40K.

Another aspect of the invention involves cross-linking the peptides of the invention to improve their pharmacokinetic, immunogenic, diagnostic, and/or therapeutic attributes. Cross-linking involves joining two molecules by a covalent bond through a chemical reaction at suitable site(s) (e.g., primary amines, sulfhydryls) on the cytokine and ligand of the invention. In an embodiment, the cytokine and ligand may be cross-linked together. The cross-linking agents may form a cleavable or non-cleavable linker between the cytokine and the ligand. Cross-linking agents that form non-cleavable linkers between the cytokine and the ligand may comprise a maleimido- or haloacetyl-based moiety. According to the present invention, such non-cleavable linkers are said to be derived from maleimido- or haloacetyl-based moiety. Cross-linking agents comprising a maleimido-based moiety include N-succinimidyl 4-(maleimidomethyl)cyclohexanecarboxylate (SMCC), N-succinimidyl-4-(N-maleimidomethyl)-cyclohexane-1-carboxy-(6-amidocaproate), which is a “long chain” analog of SMCC (LC-SMCC), κ-maleimidoundecanoic acid N-succinimidyl ester (KMUA), γ-maleimidobutyric acid N-succinimidyl ester (GMBS), ε-maleimidocaproic acid N-hydroxysuccinimide ester (EMCS), m-maleimidobenzoyl-N-hydroxysuccinimide ester (MBS), N-(α-maleimidoacetoxy)-succinimide ester [AMAS], succinimidyl-6-(β-maleimidopropionamido)hexanoate (SMPH), N-succinimidyl 4-(p-maleimidophenyl)-butyrate (SMPB), and N-(p-maleimidophenyl)isocyanate (PMPI). These cross-linking agents form non-cleavable linkers derived from maleimido-based moieties. Cross-linking agents comprising a haloacetyl-based moiety include N-succinimidyl-4-(iodoacetyl)-aminobenzoate (SIAB), N-succinimidyl iodoacetate (SIA), N-succinimidyl bromoacetate (SBA) and N-succinimidyl 3-(bromoacetamido)propionate (SBAP). These cross-linking agents form non-cleavable linkers derived from haloacetyl-based moieties. Cross-linking agents that form non-cleavable linkers between the cytokine and the ligand may comprise N-succinimidyl 3-(2-pyridyldithio)propionate, 4-succinimidyl-oxycarbonyl-α-methyl-alpha-(2-pyridyldithio)-toluene (SMPT), N-succinimidyl-3-(2-pyridyldithio)-butyrate (SDPB), 2-iminothiolane, or acetylsuccinic anhydride.

(d) Chimeric Peptide

In another aspect, the invention encompasses a chimeric peptide comprising a cytokine peptide and a NKG2D ligand peptide. In an alternate aspect, the invention encompasses a chimeric peptide comprising a cytokine peptide and a PD1 ligand peptide. It should be understood that “ligand peptide” is used interchangeably with “ligand” and “cytokine peptide” is used interchangeably with “cytokine” for purposes of descriptions herein of various cytokines and ligands that are suitable for use in the present compositions and methods. In certain embodiments, the cytokine peptide is in the IL2 subfamily. More specifically, the cytokine peptide is selected from the group consisting of IL2, IL7, IL15 and IL21. In a specific embodiment, the cytokine peptide is IL15 or a mutant thereof. In another specific embodiment, the cytokine peptide is IL2 or a mutant thereof. In another embodiment, the cytokine peptide is mutant IL2 comprising at least one mutation selected from the group consisting of R38A, F42K and C125S. In a specific embodiment, the cytokine peptide comprises the amino acid sequence set forth in SEQ ID NO:5 or SEQ ID NO:6. In other embodiments, the cytokine peptide is in the IL1 family. More specifically, the cytokine peptide is selected from the group consisting of IL1α, IL1β, IL1Ra, IL18, IL36Ra, IL36α, IL37, IL36β, IL36γ, IL38, and IL33. In a specific embodiment, the cytokine peptide is IL18 or a mutant thereof.

In certain embodiments, the cytokine peptide is in the tumor necrosis factor ligand superfamily (TNFSF). More specifically, the cytokine peptide is selected from the group consisting of TNF-alpha, OX40L, a 4-1BB ligand, TRAIL, Fas ligand, lymphotoxin-alpha, lymphotoxin-beta, CD30L, CD40L, CD27L and RANKL. In a specific embodiment, the cytokine peptide is OX40L, or a mutant thereof. In another specific embodiment, the cytokine peptide contains an OX40L fragment. In a specific embodiment, the OX40L fragment comprises the amino acid sequence set forth in SEQ ID NO:57. In certain specific embodiments, the OX40L fragments may be connected into a continuous construct via linker peptides. In a specific embodiment, the construct containing the OX40L fragments comprises the amino acid sequence set forth in SEQ ID NO:58. In certain embodiments, the cytokine peptide is a mutant OX40L comprising at least one mutant selected from the group N166A and F180A. In a specific embodiment, the cytokine contains a mutant OX40L fragment containing at least one mutant selected from the group N166A and F180A. In a specific embodiment, the mutant OX40L fragment comprises the amino acid sequence set forth in SEQ ID NO:59. In certain specific embodiments, mutant OX40L fragments or mutant and unmutated OX40L fragments may be connected into a continuous construct via linker peptides. In a specific embodiment, the construct containing the mutant and unmutated OX40L fragments comprises the amino acid sequence set forth in SEQ ID NO:60 or SEQ ID NO:61. In an alternate specific embodiment, the cytokine peptide is 4-1BBL, or a mutant thereof. In another specific embodiment, the cytokine peptide contains a 4-1BBL fragment. In a specific embodiment, the 4-1BBL fragment comprises the amino acid sequence set forth in SEQ ID NO:65. In certain specific embodiments, the 4-1BBL fragments may be connected into a continuous construct via linker peptides. In a specific embodiment, the construct containing the 4-1BBL fragments comprises the amino acid sequence set forth in SEQ ID NO:66. In certain embodiments, the cytokine peptide is a mutant 4-1BBL. In certain embodiments, the cytokine contains a mutant 4-1BBL fragment. In certain embodiments, mutant 4-1BBL fragments or mutant and unmutated 4-1BBL fragments may be connected into a continuous construct via linker peptides.

In certain embodiments, the NKG2D ligand peptide is an anti-NKG2D antibody. In another embodiment, the NKG2D ligand peptide is a MHC class-I-related glycoprotein. In another embodiment, the ligand peptide is OMCP, a portion thereof, or a mutant thereof. In an embodiment, the ligand peptide binds to a receptor expressed on NK cells and CD8⁺ CTLs. In a specific embodiment, the ligand peptide binds to an NKG2D receptor. In certain embodiments, the ligand peptide comprises the amino acid sequence set forth in SEQ ID NO:7 or a portion thereof that is capable of binding to the NKG2D receptor.

In certain embodiments, the PD1 ligand peptide is an anti-PD1 antibody. In another embodiment, the PD1 ligand peptide is PDL1, a portion thereof, or a mutant thereof. In yet another embodiment, the PD1 ligand peptide is PDL2, a portion thereof, or a mutant thereof. In an embodiment, the ligand peptide binds to a receptor expressed on T cells, NK cells, and macrophages. In a specific embodiment, the ligand peptide binds to a PD1 receptor. In certain embodiments, the ligand peptide comprises the amino acid sequence set forth in SEQ ID NO:48 or SEQ ID NO:50 or a portion thereof that is capable of binding to the PD1 receptor.

In other embodiments, a chimeric peptide further comprises a linker peptide. In certain embodiments, a linker peptide comprises the amino acid sequence selected from the group consisting of (AAS)_n, (AAAL)_n (SEQ ID NO:68), (G_nS)_n or (G₂S)_n, wherein A is alanine, S is serine, L is leucine, and G is glycine and wherein n is an integer from 1-20, or 1-10, or 3-10. In a different embodiment, a linker peptide comprises at least one tag selected from the group consisting of a FLAG tag and a His tag. In an embodiment, a linker peptide is about 20 to about 30 amino acids. In a specific embodiment, a linker peptide comprises the amino acid sequence set forth in SEQ ID NO:8.

The invention also encompasses a nucleic acid molecule encoding a chimeric peptide as described herein. Additionally, the invention encompasses a pharmaceutical composition comprising a chimeric peptide as described herein. Pharmaceutical compositions are described in more detail in Section I(h).

A chimeric peptide of the disclosure may optionally comprise a signal peptide and/or a purification moiety. When present, typically the signal peptide is at the N-terminus of the chimeric peptide and the purification moiety is at the C-terminus of the chimeric peptide. Alternatively, the signal peptide and the purification moiety are both at the N-terminus of the chimeric peptide. The choice of signal peptide can and will vary depending on a variety factors including, but not limited to, the desired cellular location and type of cell. Suitable polynucleotide sequence encoding signal peptides are known in the art, as are polypeptide sequences encoded therefrom. In a specific embodiment, the signal peptide comprises SEQ ID NO:69 (MGILPSPGMPALLSLVSLLSVLLMGCVAETG). Similarly, the choice of purification moiety can and will vary. Suitable purification moieties are known in the art, as are the polynucleotide sequences encoding them. In general, signal peptides and/or purification moieties are cleaved off during processing and not included in the final chimeric peptide for use in a pharmaceutical composition.

The disclosure also encompasses a vector comprising a nucleic acid sequence capable of encoding a chimeric peptide of the disclosure. As used herein, a “vector” is defined as a nucleic acid molecule used as a vehicle to transfer genetic material. Vectors include but are not limited to, plasmids, phasmids, cosmids, transposable elements, viruses (bacteriophage, animal viruses, and plant viruses), and artificial chromosomes (e.g., YACs), such as retroviral vectors (e.g. derived from Moloney murine leukemia virus vectors (MoMLV), MSCV, SFFV, MPSV, SNV etc), lentiviral vectors (e.g. derived from HIV-1, HIV-2, SIV, BIV, FIV etc.), adenoviral (Ad) vectors including replication competent, replication deficient and gutless forms thereof, adeno-associated viral (AAV) vectors, simian virus 40 (SV-40) vectors, bovine papilloma virus vectors, Epstein-Barr virus, herpes virus vectors, vaccinia virus vectors, Harvey murine sarcoma virus vectors, murine mammary tumor virus vectors, Rous sarcoma virus vectors. An expression vector encoding a chimeric peptide of the disclosure may be delivered to the cell using a viral vector or via a non-viral method of transfer. Viral vectors suitable for introducing nucleic acids into cells include retroviruses, adenoviruses, adeno-associated viruses, rhabdoviruses, and herpes viruses. Non-viral methods of nucleic acid transfer include naked nucleic acid, liposomes, and protein/nucleic acid conjugates. An expression construct encoding a chimeric peptide of the disclosure that is introduced to the cell may be linear or circular, may be single-stranded or double-stranded, and may be DNA, RNA, or any modification or combination thereof. The disclosure also encompasses a cell line comprising a vector comprising a nucleic acid sequence capable of encoding a chimeric peptide of the disclosure. In some embodiments, the cell line is an immortalized cell line.

(e) Targeting Molecule

As used herein, a “targeting molecule” is a molecule that is capable of binding to a target specific to a cell in a disease state or to the extracellular matrix surrounding the diseased cell. In some instances, the targeting molecule binds a target molecular entity expressed on a cell. The targeting molecule may be any molecule capable of such association or binding including, but not limited to, receptor ligands and antibodies. Various types of targeting molecules will be known to one of skill in the art. For example, receptor ligands bind to target receptors expressed on the surface of a cell. Targeting molecules may also include other molecules such as interferons alpha, beta and gamma. Other examples of targeting molecules include antibodies, including agonist and antagonist antibodies to TNF receptors, antibodies to antigens present in a tumor stroma, antibodies to mesothelin and antibodies carcinoembryonic antigen. Antibodies to particular antigen targets may be generated by means known to those skilled in the art, including those methods discussed previously in this disclosure. In certain aspects, a targeting molecule may include only a portion of a molecule such as the binding portion of a ligand or antibody. The targeting molecule may be linked to the ligand by a linker as discussed in this disclosure. The targeting molecules of the present invention may be produced by means known to those of skill in the art.

(f) Combination Therapies

As used herein, “combination” is meant to include therapies that can be administered separately, for example, formulated separately for separate administration (e.g., as can be provided in a kit), and therapies that can be administered together in a single formulation (i.e., a “co-formulation”). Combinations of the polypeptides provided herein with one or more active therapeutic agents can be administered or applied sequentially (e.g., where one agent is administered prior to one or more other agents) or simultaneously (e.g., where two or more agents are administered at or about the same time). In some embodiments, administration is sequential. In other embodiments, administration is simultaneous. Regardless of whether the two or more agents are administered sequentially or simultaneously, they are considered to be administered in combination for purposes of the present disclosure.

Accordingly, methods and uses of the polypeptides described herein can be practiced prior to, substantially contemporaneously with or following another treatment, and can be supplemented with other forms of therapy.

In an aspect, provided herein are combination therapies that include a composition as described herein and a PD-1 inhibitor. A “PD-1 inhibitor” refers to a moiety (e.g., compound, nucleic acid, polypeptide, antibody) that decreases, inhibits, blocks, abrogates or interferes with the activity or expression of PD-1 (e.g., Programmed Cell Death Protein 1; PD-1 (CD279); GI: 145559515), including variants, isoforms, species homologs of human PD-1 (e.g., mouse) and analogues that have at least one common epitope with PD-1. A PD-1 inhibitor includes molecules and macromolecules such as, for example, compounds, nucleic acids, polypeptides, antibodies, peptibodies, diabodies, minibodies, nanobodies, single-chain variable fragments (scFv), and functional fragments or variants thereof. In particular embodiments described herein, a PD-1 inhibitor is an anti-PD-1 antibody. A PD-1 inhibitor (including an anti-PD-1 antibody) can antagonize PD-1 activity or expression. An anti-PD-1 antibody can be a monoclonal or polyclonal antibody as described herein. In some embodiments, the anti-PD-1 antibody is a monoclonal antibody. In other embodiments, the anti-PD-1 antibody is a polyclonal antibody. 0).

In one embodiment, the PD-1 inhibitor is selected from the group consisting of nivolumab, pembrolizumab, pidilizumab, AMP-224, REGN2810, PDR 001, and MEDI0680. In some embodiments, the PD-1 inhibitor is nivolumab. In some embodiments, the PD-1 inhibitor is pembrolizumab. In some embodiments, the PD-1 inhibitor is pidilizumab. In some embodiments, the PD-1 inhibitor is AMP-224. In some embodiments, the PD-1 inhibitor is REGN2810. In some embodiments, the PD-1 inhibitor is PDR 001. In some embodiments, the PD-1 inhibitor is MEDI0680.

In an aspect, the invention encompasses a combination therapy that includes a PD-1 inhibitor described herein and a composition comprising a cytokine as provided herein linked to a NKG2D ligand provided herein. The composition may further comprise a linker as described herein to connect the cytokine to the ligand as provided herein. For example, the cytokine can be an IL1 family cytokine, including those described herein (e.g., IL1α, IL1β, IL1 Ra, IL18, IL36Ra, IL36α, IL37, IL36β, IL36γ, IL38, and IL33. For example, the cytokine can be an IL2 subfamily cytokine such as IL2, IL4, IL7, IL9, IL15 and IL21. In some embodiments, the cytokine is IL2. In other embodiments, the cytokine is a mutant R38A/F42K form of IL2. For example, the cytokine can be an interferon as described herein (e.g., IFN-α, IFN-β, IFN-ε, IFN-κ, IFN-ω, IL10R2, or IFNLR1). In another example the cytokine is an interleukin such as, but not limited to, IL1, IL2, IL3, IL4, IL5, IL6, IL7, IL8 (CXCL8), IL9, IL10, IL11, IL12, IL13, IL14, IL15, IL16, IL17, IL18, IL19, IL20, IL21, IL22, IL23, IL24, IL25, IL26, IL27, IL28, IL29, IL30, IL31, IL32, IL33, IL35, or IL36. In another example, the cytokine is a member of the TNFSF family such as, but not limited to TNF (TNFalpha), CD40L (TNFSF5), CD70 (TNFSF7), EDA, FASLG (TNFSF6), LTA (TNFSF1), LTB (TNFSF3), TNFSF4 (OX40L), TNFSF8 (CD153), TNFSF9 (4-1BBL), TNFSF10 (TRAIL), TNFSF11 (RANKL), TNFSF12 (TWEAK), TNFSF13, TNFSF13B, TNFSF14, TNFSF15, TNFSF18. For example, the NKG2D ligand can be NKG2A, NKG2B, NKG2C, NKG2D, NKG2E, NKG2F or NKG2H as described herein. The ligand can be selected from the group consisting of MICA, MICB, ULBP1, ULBP2, ULBP3, ULBP4, ULBP5, ULBP6, Rae1, H60a, H60b, H60c, h-HLA-A, Multi or OMCP. In certain embodiments, the NKG2D ligand is OMCP (e.g., SEQ ID NOs: 7, 13, or 14) as described herein.

In one embodiment, the combination therapy includes a PD-1 inhibitor described herein and a composition that includes OMCP or a portion thereof as provided herein and a targeting molecule. The OMCP can be linked to the targeting molecule or a portion of OMCP can be linked to the targeting molecule. In one embodiment, the combination therapy includes a PD-1 inhibitor described herein and a composition comprising OMCP or a portion thereof as provided herein and a tumor necrosis factor (TNF) family member. In one embodiment, the combination therapy includes a PD-1 inhibitor described herein and a composition comprising OMCP or a portion thereof as provided herein and TNF-related apoptosis-inducing targeting molecule. In one embodiment, the combination therapy includes a PD-1 inhibitor described herein and a composition comprising OMCP or a portion thereof as provided herein and a 4-1BB ligand. In one embodiment, the combination therapy includes a PD-1 inhibitor described herein and a composition comprising OMCP or a portion thereof as provided herein and a 4-1BB agonist. In one embodiment, the combination therapy includes a PD-1 inhibitor described herein and a composition comprising OMCP or a portion thereof as provided herein and TNF-alpha. In one embodiment, the combination therapy includes a PD-1 inhibitor described herein and a composition comprising OMCP or a portion thereof as provided herein and OX40L. In one embodiment, the combination therapy includes a PD-1 inhibitor described herein and a composition comprising OMCP or a portion thereof as provided herein and Fas ligand. In one embodiment, the combination therapy includes a PD-1 inhibitor described herein and a composition comprising OMCP or a portion thereof as provided herein and lymphotoxin-alpha (LT-a). In one embodiment, the combination therapy includes a PD-1 inhibitor described herein and a composition comprising OMCP or a portion thereof as provided herein and lymphotoxin-beta (LT-b). In one embodiment, the combination therapy includes a PD-1 inhibitor described herein and a composition comprising OMCP or a portion thereof as provided herein and CD40L. In one embodiment, the combination therapy includes a PD-1 inhibitor described herein and a composition comprising OMCP or a portion thereof as provided herein and CD27L. In one embodiment, the combination therapy includes a PD-1 inhibitor described herein and a composition comprising OMCP and receptor activator of nuclear factor kappa-B targeting molecule (RANKL).

In one embodiment, the combination therapy includes a PD-1 inhibitor described herein and a cytokine linked to an NKG2D ligand (e.g., KYK-1, an scFv of KYK-1, KYK-2 or an scFv of KYK-2). In one embodiment, the combination therapy includes a PD-1 inhibitor described herein and a cytokine linked to an NKG2D ligand, where the NKG2D ligand has the amino acid sequence set forth in SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, SEQ ID NO: 39, SEQ ID NO: 40, SEQ ID NO: 41, or SEQ ID NO: 42.

In one embodiment, the combination therapy includes a PD-1 inhibitor described herein and a fusion protein described herein (e.g. a NKG2D ligand and a cytokine). The combination therapy can include a PD-1 inhibitor described herein and a fusion protein having the amino acid sequence set forth in SEQ ID NO:43, SEQ ID NO:44, SEQ ID NO:45, or SEQ ID NO:46.

Further provided herein are combination therapies that include a PD-1 inhibitor and a chimeric peptide described herein. In one embodiment, the combination therapy includes a PD-1 inhibitor described herein and a chimeric peptide that includes a cytokine peptide as described herein and a NKG2D ligand peptide as described herein. In certain instances, the cytokine peptide can be selected from the group consisting of IL2, IL7, IL15, IL18, IL21, and mutants thereof. In one embodiment, the cytokine peptide of the combination therapy is IL or a mutant thereof (e.g., SEQ ID NO:5 or 6). The NKG2D ligand of the chimeric peptide in the combination therapies described herein includes those ligands provided herein (e.g. KYK-1, an scFv of KYK-1, KYK-2, or an scFv of KYK-2. In another example, the NKG2D ligand of the chimeric peptide of the combination therapy has the amino acid sequence set forth in SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, SEQ ID NO: 39, SEQ ID NO: 40, SEQ ID NO: 41, or SEQ ID NO: 42.

In another embodiment provided herein is a combination therapy that includes a PD-1 inhibitor provided herein and a chimeric peptide that includes a cytokine peptide and an anti-NKG2D antibody. The cytokine peptide is a cytokine as described hereinabove. The anti-NKG2D antibody is as described hereinabove.

In one embodiment, the combination therapy comprises an OMCP-IL2 fusion protein and a PD-1 inhibitor. In another embodiment, the combination therapy comprises an OMCP-IL2 fusion protein and an anti-PD-1 antibody. In some embodiments, the fusion protein further comprises a linker. In some embodiments, the IL2 is a mutant R38A/F42K form of IL2.

In one embodiment, the combination therapy comprises an OMCP-IL2 chimeric protein and a PD-1 inhibitor. In another embodiment, the combination therapy comprises an OMCP-IL2 chimeric protein and an anti-PD-1 antibody. In some embodiments, the chimeric protein further comprises a linker. In some embodiments, the IL2 is a mutant R38A/F42K form of IL2.

In other embodiments, the combination therapy comprises an anti-NKG2D antibody, IL2 and a PD1 inhibitor. In some embodiments, the combination therapy comprises an anti-NKG2D antibody, IL2 and an anti-PD1 antibody. In some embodiment, the anti-PD-1 antibody is an antagonistic antibody. In certain embodiments, the anti-NKG2D antibody is KYK-1. In other embodiments, the anti-NKG2D antibody is KYK-2. In some embodiments, the anti-NKG2D antibody and the IL2 are provided as a chimeric polypeptide. In some embodiments, the chimeric polypeptide further comprises a linker. In some embodiments, the anti-NKG2D antibody and the IL2 are provided as a fusion protein. In some embodiments, the fusion protein further comprises a linker. In some embodiments, the IL2 is a mutant R38A/F42K form of IL2.

In some embodiments, the combination therapy comprises an anti-NKG2D scFv, IL2 and a PD1 inhibitor. In some embodiments, the combination therapy comprises an anti-NKG2D scFv, IL2 and an anti-PD1 antibody. In some embodiment, the anti-PD-1 antibody is an antagonistic antibody. In certain embodiments, the anti-NKG2D scFv is a KYK-1 scFv. In other embodiments, the anti-NKG2D scFv is a KYK-2 scFv. In some embodiments, the anti-NKG2D scFv and the IL2 are provided as a chimeric polypeptide. In some embodiments, the chimeric polypeptide further comprises a linker. In some embodiments, the anti-NKG2D scFv and the IL2 are provided as a fusion protein. In some embodiments, the fusion protein further comprises a linker. In some embodiments, the IL2 is a mutant R38A/F42K form of IL2.

In another aspect of the invention provided herein are combination therapies that include a composition as described herein and a PD-L1 inhibitor. The term “PD-L1 inhibitor” refers to a moiety (e.g., compound, nucleic acid, polypeptide, antibody) that decreases, inhibits, blocks, abrogates or interferes with the activity, binding of PD-L1 to its receptor, PD-L1, or expression of PD-L1 (e.g., Programmed Cell Death 1 Ligand; PD-L1 (CD274); GI: 30088843), including variants, isoforms, species homologs of human PD-L1 (e.g., mouse) and analogues that have at least one common epitope with PD-L1. A PD-L1 inhibitor includes molecules and macromolecules such as, for example, compounds (small molecule compounds), nucleic acids, polypeptides, antibodies, peptibodies, diabodies, minibodies, single-domain antibodies or nanobodies, single-chain variable fragments (ScFv), and fragments or variants thereof. In particular embodiments, a PD-L1 inhibitor is an anti-PD-L1 antibody. A PD-L1 inhibitor (including an anti-PD-L1 antibody) can antagonize PD-L1 activity, its binding to PD-1, or its expression. Exemplary PD-L1 inhibitors include, but are not limited to, durvalumab, avelumab, atezolizumab, BMS-936559, STI-A1010, STI-A1011, STI-A1012, STI-A1013, STI-A1014, and STI-A1015.

In an aspect, the invention encompasses a combination therapy that includes a PD-L1 inhibitor described herein and a composition comprising a cytokine as provided herein linked to a NKG2D ligand provided herein. In some embodiments, the PD-L1 inhibitor is durvalumab. In some embodiments, the PD-L1 inhibitor is avelumab. In some embodiments, the PD-L1 inhibitor is atezolizumab. In some embodiments, the PD-L1 inhibitor is BMS-936559. In some embodiments, the PD-L1 inhibitor is STI-A1010, STI-A1011, STI-A1012, STI-A1013, STI-A1014, or STI-A1015.

The composition may further comprise a linker as described herein to connect the cytokine to the ligand as provided herein. The cytokine is a cytokine described herein. For example, the cytokine can be an IL1 family cytokine, including those described herein (e.g., IL1α, IL1β, IL1 Ra, IL18, IL36Ra, IL36α, IL37, IL36β, IL36γ, IL38, and IL33. For example, the cytokine can be an IL2 subfamily cytokine such as IL2, IL4, IL7, IL9, IL15 and IL21. In some embodiments, the cytokine is IL2. In other embodiments, the cytokine is a mutant R38A/F42K form of IL2. For example, the cytokine can be an interferon as described herein (e.g., IFN-α, IFN-β, IFN-ε, IFN-κ, IFN-ω, IL10R2, or IFNLR1). In another example the cytokine is an interleukin such as, but not limited to, IL1, IL2, IL3, IL4, IL5, IL6, IL7, IL8 (CXCL8), IL9, IL10, IL11, IL12, IL13, IL14, IL15, IL16, IL17, IL18, IL19, IL20, IL21, IL22, IL23, IL24, IL25, IL26, IL27, IL28, IL29, IL30, IL31, IL32, IL33, IL35, or IL36. In another example, the cytokine is a member of the TNFSF family such as, but not limited to TNF (TNFalpha), CD40L (TNFSF5), CD70 (TNFSF7), EDA, FASLG (TNFSF6), LTA (TNFSF1), LTB (TNFSF3), TNFSF4 (OX40L), TNFSF8 (CD153), TNFSF9 (4-1BBL), TNFSF10 (TRAIL), TNFSF11 (RANKL), TNFSF12 (TWEAK), TNFSF13, TNFSF13B, TNFSF14, TNFSF15, TNFSF18. The NKG2D ligand is as described above. For example, the ligand can be NKG2A, NKG2B, NKG2C, NKG2D, NKG2E, NKG2F or NKG2H as described herein. The ligand can be selected from the group consisting of MICA, MICB, ULBP1, ULBP2, ULBP3, ULBP4, ULBP5, ULBP6, Rae1, H60a, H60b, H60c, h-HLA-A, Multi or OMCP. In certain instances the NKG2D ligand is OMCP (e.g., SEQ ID NOs: 7, 13, or 14) as described herein.

In one embodiment, the combination therapy includes a PD-L1 inhibitor described herein and a composition that includes OMCP or a portion thereof as provided herein and a targeting molecule. The OMCP can be linked to the targeting molecule or a portion of OMCP can be linked to the targeting molecule. In one embodiment, the combination therapy includes a PD-L1 inhibitor described herein and a composition comprising OMCP or a portion thereof as provided herein and a tumor necrosis factor (TNF) family member. In one embodiment, the combination therapy includes a PD-L1 inhibitor described herein and a composition comprising OMCP or a portion thereof as provided herein and TNF-related apoptosis-inducing targeting molecule. In one embodiment, the combination therapy includes a PD-L1 inhibitor described herein and a composition comprising OMCP or a portion thereof as provided herein and a 4-1BB ligand. In one embodiment, the combination therapy includes a PD-L1 inhibitor described herein and a composition comprising OMCP or a portion thereof as provided herein and a 4-1BB agonist. In one embodiment, the combination therapy includes a PD-L1 inhibitor described herein and a composition comprising OMCP or a portion thereof as provided herein and TNF-alpha. In one embodiment, the combination therapy includes a PD-L1 inhibitor described herein and a composition comprising OMCP or a portion thereof as provided herein and OX40L. In one embodiment, the combination therapy includes a PD-L1 inhibitor described herein and a composition comprising OMCP or a portion thereof as provided herein and Fas ligand. In one embodiment, the combination therapy includes a PD-L1 inhibitor described herein and a composition comprising OMCP or a portion thereof as provided herein and lymphotoxin-alpha (LT-a). In one embodiment, the combination therapy includes a PD-L1 inhibitor described herein and a composition comprising OMCP or a portion thereof as provided herein and lymphotoxin-beta (LT-b). In one embodiment, the combination therapy includes a PD-L1 inhibitor described herein and a composition comprising OMCP or a portion thereof as provided herein and CD40L. In one embodiment, the combination therapy includes a PD-L1 inhibitor described herein and a composition comprising OMCP or a portion thereof as provided herein and CD27L. In one embodiment, the combination therapy includes a PD-L1 inhibitor described herein and a composition comprising OMCP and receptor activator of nuclear factor kappa-B targeting molecule (RANKL).

In one embodiment, the combination therapy includes a PD-L1 inhibitor described herein and a cytokine linked to an NKG2D ligand (e.g., KYK-1, an scFv of KYK-1, KYK-2 or an scFv of KYK-2). In one embodiment, the combination therapy includes a PD-L1 inhibitor described herein and a cytokine linked to an NKG2D ligand, where the NKG2D ligand has the amino acid sequence set forth in SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, SEQ ID NO: 39, SEQ ID NO: 40, SEQ ID NO: 41, or SEQ ID NO: 42.

In one embodiment, the combination therapy includes a PD-L1 inhibitor described herein and a fusion protein described herein (e.g. a NKG2D ligand and a cytokine). The combination therapy can include a PD-L1 inhibitor described herein and a fusion protein having the amino acid sequence set forth in SEQ ID NO:43, SEQ ID NO:44, SEQ ID NO:45, or SEQ ID NO:46.

Further provided herein are combination therapies that include a PD-L1 inhibitor and a chimeric peptide described herein. In one embodiment, the combination therapy includes a PD-L1 inhibitor described herein and a chimeric peptide that includes a cytokine peptide as described herein and a NKG2D ligand peptide as described herein. In certain instances, the cytokine peptide can be selected from the group consisting of IL2, IL7, IL15, IL18, IL21, and mutants thereof. In one embodiment, the cytokine peptide of the combination therapy is IL or a mutant thereof (e.g., SEQ ID NO:5 or 6). The NKG2D ligand of the chimeric peptide in the combination therapies described herein includes those ligands provided herein (e.g. KYK-1, an scFv of KYK-1, KYK-2, or an scFv of KYK-2. In another example, the NKG2D ligand of the chimeric peptide of the combination therapy has the amino acid sequence set forth in SEQ ID NO: 35, SEQ ID NO: 36, SEQ ID NO: 37, SEQ ID NO: 38, SEQ ID NO: 39, SEQ ID NO: 40, SEQ ID NO: 41, or SEQ ID NO: 42.

In another embodiment provided herein is a combination therapy that includes a PD-L1 inhibitor provided herein and a chimeric peptide that includes a cytokine peptide and an anti-NKG2D antibody. The cytokine peptide is a cytokine as described hereinabove. The anti-NKG2D antibody is as described hereinabove.

In another embodiment provided herein is a combination therapy that includes a PD-L1 inhibitor provided herein and a chimeric peptide that includes a cytokine peptide and an anti-NKG2D antibody. The cytokine peptide is a cytokine as described hereinabove. The anti-NKG2D antibody is as described hereinabove.

In one embodiment, the combination therapy comprises an OMCP-IL2 fusion protein and a PD-L1 inhibitor. In another embodiment, the combination therapy comprises an OMCP-IL2 fusion protein and an anti-PD-L1 antibody. In some embodiments, the fusion protein further comprises a linker. In some embodiments, the IL2 is a mutant R38A/F42K form of IL2.

In one embodiment, the combination therapy comprises an OMCP-IL2 chimeric protein and a PD-L1 inhibitor. In another embodiment, the combination therapy comprises an OMCP-IL2 chimeric protein and an anti-PD-L1 antibody. In some embodiments, the chimeric protein further comprises a linker. In some embodiments, the IL2 is a mutant R38A/F42K form of IL2.

In other embodiments, the combination therapy comprises an anti-NKG2D antibody, IL2 and a PD1 inhibitor. In some embodiments, the combination therapy comprises an anti-NKG2D antibody, IL2 and an anti-PD1 antibody. In some embodiment, the anti-PD-L1 antibody is an antagonistic antibody. In certain embodiments, the anti-NKG2D antibody is KYK-1. In other embodiments, the anti-NKG2D antibody is KYK-2. In some embodiments, the anti-NKG2D antibody and the IL2 are provided as a chimeric polypeptide. In some embodiments, the chimeric polypeptide further comprises a linker. In some embodiments, the anti-NKG2D antibody and the IL2 are provided as a fusion protein. In some embodiments, the fusion protein further comprises a linker. In some embodiments, the IL2 is a mutant R38A/F42K form of IL2.

In some embodiments, the combination therapy comprises an anti-NKG2D scFv, IL2 and a PD1 inhibitor. In some embodiments, the combination therapy comprises an anti-NKG2D scFv, IL2 and an anti-PD1 antibody. In some embodiment, the anti-PD-L1 antibody is an antagonistic antibody. In certain embodiments, the anti-NKG2D scFv is a KYK-1 scFv. In other embodiments, the anti-NKG2D scFv is a KYK-2 scFv. In some embodiments, the anti-NKG2D scFv and the IL2 are provided as a chimeric polypeptide. In some embodiments, the chimeric polypeptide further comprises a linker. In some embodiments, the anti-NKG2D scFv and the IL2 are provided as a fusion protein. In some embodiments, the fusion protein further comprises a linker. In some embodiments, the IL2 is a mutant R38A/F42K form of IL2.

(g) Preferred Embodiments

By way of non-limiting example, several preferred compositions of the invention are depicted in FIG. 23 . 1. depicts a composition comprising α2 domain (H2) of OMCP linked to a cytokine. 2. depicts a composition comprising OMCP linked to a cytokine, wherein the composition is pegylated. 3. depicts a composition comprising OMCP linked to a cytokine, wherein the composition comprises N-glycan. 4. depicts a composition comprising, OMCP linked to a cytokine, wherein the linker comprises various sequences and various lengths. 5. depicts a composition comprising a Fab specific antibody for NKG2D linked to a cytokine. 6. depicts a composition comprising various NKG2D ligands linked to a cytokine. 7. depicts a composition comprising a mutated version of OMCP linked to a cytokine, wherein the OMCP may be mutated to have improved binding affinity or weaker binding affinity. 8. depicts a composition comprising a mutated version of OMCP linked to a cytokine, wherein the OMCP may be mutated to have binding affinity for other NKG2 receptors. 9. depicts a composition comprising a viral protein liked to a cytokine. For example, OMCP binds to NKG2D. Additionally, CPXV203 binds to MHCI. 10. depicts a composition comprising OMCP linked to a mutated cytokine. It is understood that the OMCP sequence could be from various sources such as cowpox or monkeypox. Also, Fc-chimeras of OMCP and IL2, and variants thereof may be used.

In a preferred embodiment, the composition comprises IL2, IL15 or IL18 linked to OMCP. In another preferred embodiment, the composition comprises IL2, IL15 or IL18 linked to OMCP via a peptide linker. In still another preferred embodiment, the composition comprises IL2, IL15 or IL18 linked to OMCP via a peptide linker comprising about 20 to about 30 amino acids. In still yet another preferred embodiment, the composition comprises IL2, IL15 or IL18 linked to OMCP via a peptide linker comprising a FLAG tag and a His tag. In each of the foregoing embodiments, the IL2 may be a mutated version of IL2 comprising the mutations R38A and F42K.

In a preferred embodiment, the composition comprises IL2, IL15 or IL18 linked to an anti-NKG2D antibody. In another preferred embodiment, the composition comprises IL2, IL15 or IL18 linked to an anti-NKG2D antibody via a peptide linker. In still another preferred embodiment, the composition comprises IL2, IL15 or IL18 linked to an anti-NKG2D antibody via a peptide linker comprising about 20 to about 30 amino acids. In still yet another preferred embodiment, the composition comprises IL2, IL15 or IL18 linked to an anti-NKG2D antibody via a peptide linker comprising a FLAG tag and a His tag. In each of the foregoing embodiments, the IL2 may be a mutated version of IL2 comprising the mutations R38A and F42K.

In a different preferred embodiment, the composition comprises IL2 linked to OMCP. In another preferred embodiment, the composition comprises IL2 linked to OMCP via a peptide linker. In still another preferred embodiment, the composition comprises IL2 linked to OMCP via a peptide linker comprising about 20 to about 30 amino acids. In still yet another preferred embodiment, the composition comprises IL2 linked to OMCP via a peptide linker comprising a FLAG tag and a His tag. In each of the foregoing embodiments, the IL2 may be a mutated version of IL2 comprising the mutations R38A and F42K.

In a different preferred embodiment, the composition comprises IL2 linked to an anti-NKG2D antibody. In another preferred embodiment, the composition comprises IL2 linked to an anti-NKG2D antibody via a peptide linker. In still another preferred embodiment, the composition comprises IL2 linked to an anti-NKG2D antibody via a peptide linker comprising about 20 to about 30 amino acids. In still yet another preferred embodiment, the composition comprises IL2 linked to an anti-NKG2D antibody via a peptide linker comprising a FLAG tag and a His tag. In each of the foregoing embodiments, the IL2 may be a mutated version of IL2 comprising the mutations R38A and F42K.

In an exemplary embodiment, the NKG2D ligand is an anti-NKG2D antibody or a scFv thereof, such as KYK-1 antibody, KYK-2 antibody, KYK-1 scFv, or KYK-2 scFv. In one particular exemplary embodiment, a chimeric peptide is provided wherein the anti-NKG2D antibody is KYK-1 linked to mutIL2 and comprises the amino acid sequence set forth in

SEQ ID NO: 43

(QPVLTQPSSVSVAPGETARIPCGGDDIETKSVHWYQQKPGQAPVLVIYD

DDDRPSGIPERFFGSNSGNTATLSISRVEAGDEADYYCQVWDDNNDEWVF

GGGTQLTVLGGGGSGGGGSGGGGSGGGGSEVQLVESGGGVVQPGGSLRLS

CAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTIS

RDNSKNTLYLQMNSLRAEDTAVYYCAKDRFGYYLDYWGQGTLVTVSSGGS

SGSSGSSHHHHHHHHGGSSGSSGSSAPTSSSTKKTQLQLEHLLLDLQMIL

NGINNYKNPKLTAMLTKKFYMPKKATELKHLQCLEEELKPLEEVLNLAQS

KNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFS

QSIISTLT),

or alternatively, comprises the amino acid sequence set forth in

SEQ ID NO: 44

(EVQLVESGGGVVQPGGSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVA

FIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAKD

RFGYYLDYWGQGTLVTVSSGGGGSGGGGSGGGGSGGGGSQPVLTQPSSVS

VAPGETARIPCGGDDIETKSVHWYQQKPGQAPVLVIYDDDDRPSGIPERF

FGSNSGNTATLSISRVEAGDEADYYCQVWDDNNDEWVFGGGTQLTVLGGS

SGSSGSSHHHHHHHHGGSSGSSGSSAPTSSSTKKTQLQLEHLLLDLQMIL

NGINNYKNPKLTAMLTKKFYMPKKATELKHLQCLEEELKPLEEVLNLAQS

KNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFS

QSIISTLT).

In another particular exemplary embodiment, a chimeric peptide is provided wherein the anti-NKG2D antibody is KYK-2 linked to mutIL2 and comprises the amino acid sequence set forth in

SEQ ID NO: 45

(QSALTQPASVSGSPGQSITISCSGSSSNIGNNAVNWYQQLPGKAPKLLI

YYDDLLPSGVSDRFSGSKSGTSAFLAISGLQSEDEADYYCAAWDDSLNGP

VFGGGTKLTVLGGGGSGGGGSGGGGSGGGGSQVQLVESGGGLVKPGGSLR

LSCAASGFTFSSYGMHWVRQAPGKGLEWVAFIRYDGSNKYYADSVKGRFT

ISRDNSKNTLYLQMNSLRAEDTAVYYCAKDRGLGDGTYFDYWGQGTTVTV

SSGGSSGSSGSSHHHHHHHHGGSSGSSGSSAPTSSSTKKTQLQLEHLLLD

LQMILNGINNYKNPKLTAMLTKKFYMPKKATELKHLQCLEEELKPLEEVL

NLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNR

WITFSQSIISTLT),

or alternatively, comprises the amino acid sequence set forth in

SEQ ID NO: 46

(QVQLVESGGGLVKPGGSLRLSCAASGFTFSSYGMHWVRQAPGKGLEWVA

FIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCAKD

RGLGDGTYFDYWGQGTTVTVSSGGGGSGGGGSGGGGSGGGGSQSALTQPA

SVSGSPGQSITISCSGSSSNIGNNAVNWYQQLPGKAPKLLIYYDDLLPSG

VSDRFSGSKSGTSAFLAISGLQSEDEADYYCAAWDDSLNGPVFGGGTKLT

VLGGSSGSSGSSHHHHHHHHGGSSGSSGSSAPTSSSTKKTQLQLEHLLLD

LQMILNGINNYKNPKLTAMLTKKFYMPKKATELKHLQCLEEELKPLEEVL

NLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNR

WITFSQSIISTLT).

In an exemplary embodiment, the composition comprises the DNA sequence set forth in

SEQ ID NO: 10)

(CACAAACTCGCATTCAACTTCAATCTAGAAATAAATGGCAGTGATACAC

ATTCTACAGTAGATGTATATCTTGATGATTCTCAAATTATAACGTTTGAT

GGAAAAGATATCCGTCCAACCATCCCGTTCATGATAGGTGATGAAATTTT

CTTACCGTTTTATAAAAATGTGTTTAGTGAGTTTTTCTCTCTGTTTAGAA

GAGTTCCTACAAGTACTCCATATGAAGACTTGACATATTTTTATGAATGC

GACTATACAGACAATAAATCTACATTTGATCAGTTTTATCTTTATAATGG

CGAAGAATATACTGTCAAAACACAGGAGGCCACTAATAAAAATATGTGGC

TAACTACTTCCGAGTTTAGACTAAAAAAATGGTTCGATGGCGAAGATTGT

ATAATGCATCTTAGATCGTTAGTTAGAAAAATGGAGGACAGTAAACGAAA

CACTGGTGGTACCGGAAGTAGCGGTAGTAGTGATTACAAGGACGATGACG

ACAAGCACCACCATCATCATCATCACCACGGTAGCAGCGGCAGCAGTGCC

CCCACCTCTAGCAGCACAAAGAAGACCCAGCTGCAACTGGAACACCTCCT

GCTGGACCTGCAGATGATCCTGAACGGCATCAACAACTACAAGAACCCCA

AGCTGACCGCCATGCTGACCAAAAAGTTTTACATGCCCAAGAAGGCCACC

GAGCTTAAACACCTGCAATGCCTTGAGGAGGAGCTGAAGCCCTGGAGGAG

GTACTGAACCTGGCCCAGAGCAAGAACTTTCATCTGAGGCCCAGGGACCT

GATTAGCAACATCAACGTGATCGTGTTGGAGTTGAAGGGCAGCGAGACCA

CGTTCATGTGCGAGTACGCCGACGAGACGGCCACCATAGTGGAGTTTCTT

AACAGGTGGATCACCTTCTCACAGTCTATCATCAGCACCCTGACC).

In another exemplary embodiment, the composition comprises the amino acid sequence set forth in

SEQ ID NO: 20)

(HKLAFNFNLEINGSDTHSTVDVYLDDSQIITFDGKDIRPTIPFMIGDEI

FLPFYKNVFSEFFSLFRRVPTSTPYEDLTYFYECDYTDNKSTFDQFYLYN

GEEYTVKTQEATNKNMWLTTSEFRLKKWFDGEDCIMHLRSLVRKMEDSKR

NTGGTGSSGSSDYKDDDDKHHHHHHHHGSSGSSAPTSSSTKKTQLQLEHL

LLDLQMILNGINNYKNPKLTAMLTKKFYMPKKATELKHLQCLEEELKPLE

EVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEF

LNRWITFSQSIISTLT).

In a preferred embodiment, the composition comprises OX40L or 4-1BBL, or fragment constructs thereof, linked to OMCP. In another preferred embodiment, the composition comprises OX40L or 4-1BBL, or fragment constructs thereof, linked to OMCP via a peptide linker. In still another preferred embodiment, the composition comprises OX40L or 4-1BBL, or fragment constructs thereof, linked to OMCP via a peptide linker comprising about 20 to about 30 amino acids. In still yet another preferred embodiment, the composition comprises OX40L or 4-1BBL, or fragment constructs thereof, linked to OMCP via a peptide linker comprising a FLAG tag and a His tag. In each of the foregoing embodiments, the OX40L, or fragment constructs thereof, may be a mutated version of OX40L comprising the mutations N166A and F180A.

In a preferred embodiment, the composition comprises OX40L or 4-1BBL, or fragment constructs thereof, linked to an anti-NKG2D antibody. In another preferred embodiment, the composition comprises OX40L or 4-1BBL, or fragment constructs thereof, linked to an anti-NKG2D antibody via a peptide linker. In still another preferred embodiment, the composition comprises OX40L or 4-1BBL, or fragment constructs thereof, linked to an anti-NKG2D antibody via a peptide linker comprising about 20 to about 30 amino acids. In still yet another preferred embodiment, the composition comprises OX40L or 4-1BBL, or fragment constructs thereof, linked to an anti-NKG2D antibody via a peptide linker comprising a FLAG tag and a His tag. In each of the foregoing embodiments, the OX40L, or fragment constructs thereof, may be a mutated version of OX40L comprising the mutations N166A and F180A.

In a different preferred embodiment, the composition comprises OX40L, or fragment constructs thereof, linked to OMCP. In another preferred embodiment, the composition comprises OX40L, or fragment constructs thereof, linked to OMCP via a peptide linker. In still another preferred embodiment, the composition comprises OX40L, or fragment constructs thereof, linked to OMCP via a peptide linker comprising about 20 to about 30 amino acids. In still yet another preferred embodiment, the composition comprises OX40L, or fragment constructs thereof, linked to OMCP via a peptide linker comprising a FLAG tag and a His tag. In each of the foregoing embodiments, the OX40L, or fragment constructs thereof, may be a mutated version of OX40L comprising the mutations N166A and F180A.

In a preferred embodiment, the composition comprises OX40L, or fragment constructs thereof, linked to an anti-NKG2D antibody. In another preferred embodiment, the composition comprises OX40L, or fragment constructs thereof, linked to an anti-NKG2D antibody via a peptide linker. In still another preferred embodiment, the composition comprises OX40L, or fragment constructs thereof, linked to an anti-NKG2D antibody via a peptide linker comprising about 20 to about 30 amino acids. In still yet another preferred embodiment, the composition comprises OX40L, or fragment constructs thereof, linked to an anti-NKG2D antibody via a peptide linker comprising a FLAG tag and a His tag. In each of the foregoing embodiments, the OX40L, or fragment constructs thereof, may be a mutated version of OX40L comprising the mutations N166A and F180A.

In an exemplary embodiment, the NKG2D ligand is OMCP. In an exemplary embodiment, the cytokine is OX40L. In a particular exemplary embodiment, the cytokine is a construct comprising OX40L fragments. In a particular exemplary embodiment, the OX40L fragments are combined into a continuous construct. In one particular exemplary embodiment, a chimeric peptide is provided wherein OMCP is linked to an OX40L construct via a linker peptide and comprises the amino acid sequence set forth in

SEQ ID NO: 62

(HKLAFNFNLEINGSDTHSTVDVYLDDSQIITFDGKDIRPTIPFMIGDEIF

LPFYKNVFSEFFSLFRRVPTSTPYEDLTYFYECDYTDNKSTFDQFYLYNGE

EYTVKTQEATNKNMWLTTSEFRLKKWFDGEDCIMHLRSLVRKMEDSKRNTG

GGSSGSSGSSHHHHHHHHGGSSGSSGSSGGQVSHRYPRIQSIKVQFTEYKK

EKGFILTSQKEDEIMKVQNNSVIINCDGFYLISLKGYFSQEVNISLHYQKD

EEPLFQLKKVRSVNSLMVASLTYKDKVYLNVTTDNTSLDDFHVNGGELILI

HQNPGEFCVLGGSGGGSGGGSGQVSHRYPRIQSIKVQFTEYKKEKGFILTS

QKEDEIMKVQNNSVIINCDGFYLISLKGYFSQEVNISLHYQKDEEPLFQLK

KVRSVNSLMVASLTYKDKVYLNVTTDNTSLDDFHVNGGELILIHQNPGEFC

VLGGSGGGSGGGSGQVSHRYPRIQSIKVQFTEYKKEKGFILTSQKEDEIMK

VQNNSVIINCDGFYLISLKGYFSQEVNISLHYQKDEEPLFQLKKVRSVNSL

MVASLTYKDKVYLNVTTDNTSLDDFHVNGGELILIHQNPGEFCVL).

In a particular exemplary embodiment, the cytokine is a construct comprising mutated OX40L fragments containing mutations at amino acid positions N166A and F180A. In a particular exemplary embodiment, the mutated OX40L fragments are combined into a continuous construct, with or without unmutated OX40L fragments. In one particular exemplary embodiment, a chimeric peptide is provided wherein OMCP is linked to a mutated OX40L construct via a linker peptide and comprises the amino acid sequence set forth in

SEQ ID NO: 63

(HKLAFNFNLEINGSDTHSTVDVYLDDSQIITFDGKDIRPTIPFMIGDEIF

LPFYKNVFSEFFSLFRRVPTSTPYEDLTYFYECDYTDNKSTFDQFYLYNGE

EYTVKTQEATNKNMWLTTSEFRLKKWFDGEDCIMHLRSLVRKMEDSKRNTG

GGSSGSSGSSHHHHHHHHGGSSGSSGSSGGQVSHRYPRIQSIKVQFTEYKK

EKGFILTSQKEDEIMKVQNNSVIINCDGFYLISLKGYFSQEVNISLHYQKD

EEPLFQLKKVRSVNSLMVASLTYKDKVYLNVTTDNTSLDDFHVAGGELILI

HQNPGEACVLGGSGGGSGGGSGQVSHRYPRIQSIKVQFTEYKKEKGFILTS

QKEDEIMKVQNNSVIINCDGFYLISLKGYFSQEVNISLHYQKDEEPLFQLK

KVRSVNSLMVASLTYKDKVYLNVTTDNTSLDDFHVAGGELILIHQNPGEAC

VLGGSGGGSGGGSGQVSHRYPRIQSIKVQFTEYKKEKGFILTSQKEDEIMK

VQNNSVIINCDGFYLISLKGYFSQEVNISLHYQKDEEPLFQLKKVRSVNSL

MVASLTYKDKVYLNVTTDNTSLDDFHVNGGELILIHQNPGEFCVL)

or

SEQ ID NO: 64

(HKLAFNFNLEINGSDTHSTVDVYLDDSQIITFDGKDIRPTIPFMIGDEIF

LPFYKNVFSEFFSLFRRVPTSTPYEDLTYFYECDYTDNKSTFDQFYLYNGE

EYTVKTQEATNKNMWLTTSEFRLKKWFDGEDCIMHLRSLVRKMEDSKRNTG

GGSSGSSGSSHHHHHHHHGGSSGSSGSSGGQVSHRYPRIQSIKVQFTEYKK

EKGFILTSQKEDEIMKVQNNSVIINCDGFYLISLKGYFSQEVNISLHYQKD

EEPLFQLKKVRSVNSLMVASLTYKDKVYLNVTTDNTSLDDFHVAGGELILI

HQNPGEACVLGGSGGGSGGGSGQVSHRYPRIQSIKVQFTEYKKEKGFILTS

QKEDEIMKVQNNSVIINCDGFYLISLKGYFSQEVNISLHYQKDEEPLFQLK

KVRSVNSLMVASLTYKDKVYLNVTTDNTSLDDFHVNGGELILIHQNPGEFC

VLGGSGGGSGGGSGQVSHRYPRIQSIKVQFTEYKKEKGFILTSQKEDEIMK

VQNNSVIINCDGFYLISLKGYFSQEVNISLHYQKDEEPLFQLKKVRSVNSL

MVASLTYKDKVYLNVTTDNTSLDDFHVNGGELILIHQNPGEFCVL).

In a different preferred embodiment, the composition comprises 4-1BBL, or fragment constructs thereof, linked to OMCP. In another preferred embodiment, the composition comprises 4-1BBL, or fragment constructs thereof, linked to OMCP via a peptide linker. In still another preferred embodiment, the composition comprises 4-1BBL, or fragment constructs thereof, linked to OMCP via a peptide linker comprising about 20 to about 30 amino acids. In still yet another preferred embodiment, the composition comprises 4-1BBL, or fragment constructs thereof, linked to OMCP via a peptide linker comprising a FLAG tag and a His tag.

In a different preferred embodiment, the composition comprises 4-1BBL, or fragment constructs thereof, linked to an anti-NKG2D antibody. In another preferred embodiment, the composition comprises 4-1BBL, or fragment constructs thereof, linked to an anti-NKG2D antibody via a peptide linker. In still another preferred embodiment, the composition comprises 4-1BBL, or fragment constructs thereof, linked to an anti-NKG2D antibody via a peptide linker comprising about 20 to about 30 amino acids. In still yet another preferred embodiment, the composition comprises 4-1BBL, or fragment constructs thereof, linked to an anti-NKG2D antibody via a peptide linker comprising a FLAG tag and a His tag.

In an exemplary embodiment, the NKG2D ligand is OMCP. In an exemplary embodiment, the cytokine is 4-1BBL. In a particular exemplary embodiment, the cytokine is a construct comprising 4-1BBL fragments. In a particular exemplary embodiment, the 4-1BBL fragments are combined into a continuous construct. In one particular exemplary embodiment, a chimeric peptide is provided wherein OMCP is linked to an 4-1BBL construct via a linker peptide and comprises the amino acid sequence set forth in

SEQ ID NO: 67

(HKLAFNFNLEINGSDTHSTVDVYLDDSQIITFDGKDIRPTIPFMIGDEIF

LPFYKNVFSEFFSLFRRVPTSTPYEDLTYFYECDYTDNKSTFDQFYLYNGE

EYTVKTQEATNKNMWLTTSEFRLKKWFDGEDCIMHLRSLVRKMEDSKRNTG

GGSSGSSGSSHHHHHHHHGGSSGSSGSSGGACPWAVSGARASPGSAASPRL

REGPELSPDDPAGLLDLRQGMFAQLVAQNVLLIDGPLSWYSDPGLAGVSLT

GGLSYKEDTKELVVAKAGVYYVFFQLELRRVVAGEGSGSVSLALHLQPLRS

AAGAAALALTVDLPPASSEARNSAFGFQGRLLHLSAGQRLGVHLHTEARAR

HAWQLTQGATVLGLFRVTPEIPAGLPSPRSEGGSGGGSGGGSGACPWAVSG

ARASPGSAASPRLREGPELSPDDPAGLLDLRQGMFAQLVAQNVLLIDGPLS

WYSDPGLAGVSLTGGLSYKEDTKELVVAKAGVYYVFFQLELRRVVAGEGSG

SVSLALHLQPLRSAAGAAALALTVDLPPASSEARNSAFGFQGRLLHLSAGQ

RLGVHLHTEARARHAWQLTQGATVLGLFRVTPEIPAGLPSPRSEGGSGGGS

GGGSGACPWAVSGARASPGSAASPRLREGPELSPDDPAGLLDLRQGMFAQL

VAQNVLLIDGPLSWYSDPGLAGVSLTGGLSYKEDTKELVVAKAGVYYVFFQ

LELRRVVAGEGSGSVSLALHLQPLRSAAGAAALALTVDLPPASSEARNSAF

GFQGRLLHLSAGQRLGVHLHTEARARHAWQLTQGATVLGLFRVTPEIPAGL

PSPRSE).

In another preferred embodiment, a composition comprises OMCP or a portion thereof and a targeting molecule. In another preferred embodiment, the OMCP or a portion thereof is linked to the targeting molecule via a linker. In still yet another preferred embodiment, the portion of OMCP comprises the H2b an activating portion of OMCP. In particular preferred embodiments, the activating portion of OMCP comprises the H2B helix.

In another non-limiting example, several preferred compositions of the invention binding the PD1 receptor are depicted in FIG. 36 .

In a preferred embodiment, the composition comprises IL2, IL15 or IL18 linked to PDL1. In another preferred embodiment, the composition comprises IL2, IL15 or IL18 linked to PDL1 via a peptide linker. In still another preferred embodiment, the composition comprises IL2, IL15 or IL18 linked to PDL1 via a peptide linker comprising about 20 to about 30 amino acids. In still yet another preferred embodiment, the composition comprises IL2, IL15 or IL18 linked to PDL1 via a peptide linker comprising a FLAG tag and a His tag. In each of the foregoing embodiments, the IL2 may be a mutated version of IL2 comprising the mutations R38A and F42K.

In another preferred embodiment, the composition comprises IL2, IL15 or IL18 linked to PDL2. In another preferred embodiment, the composition comprises IL2, IL15 or IL18 linked to PDL2 via a peptide linker. In still another preferred embodiment, the composition comprises IL2, IL15 or IL18 linked to PDL2 via a peptide linker comprising about 20 to about 30 amino acids. In still yet another preferred embodiment, the composition comprises IL2, IL15 or IL18 linked to PDL2 via a peptide linker comprising a FLAG tag and a His tag. In each of the foregoing embodiments, the IL2 may be a mutated version of IL2 comprising the mutations R38A and F42K.

In yet another preferred embodiment, the composition comprises IL2, IL15 or IL18 linked to an anti-PD1 antibody. In another preferred embodiment, the composition comprises IL2, IL15 or IL18 linked to an anti-PD1 antibody via a peptide linker. In still another preferred embodiment, the composition comprises IL2, IL15 or IL18 linked to an anti-PD1 antibody via a peptide linker comprising about 20 to about 30 amino acids. In still yet another preferred embodiment, the composition comprises IL2, IL15 or IL18 linked to an anti-PD1 antibody via a peptide linker comprising a FLAG tag and a His tag. In each of the foregoing embodiments, the IL2 may be a mutated version of IL2 comprising the mutations R38A and F42K.

In an exemplary embodiment, the PD1 ligand is PDL1. In one particular exemplary embodiment, a chimeric peptide is provided wherein the PD1 ligand is PDL1 linked to mutIL2 and comprises the amino acid sequence set forth in

SEQ ID NO: 48

(AFTVTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNIIQF

VHGEEDLKVQHSSYRQRARLLKDQLSLGNAALQITDVKLQDAGVYRCMISY

GGADYKRITVKVNAPYGGSSGSSGSSHHHHHHHHGGSSGSSGSSGGAPTSS

STKKTQLQLEHLLLDLQMILNGINNYKNPKLTAMLTKKFYMPKKATELKHL

QCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEY

ADETATIVEFLNRWITFSQSIISTLT).

In a particular exemplary embodiment, the composition comprises the DNA sequence set forth in

SEQ ID NO: 47

(GCCTTCACCGTGACTGTGCCCAAGGATCTGTACGTCGTGGAGTACGGCTC

CAACATGACAATCGAGTGCAAGTTCCCCGTGGAGAAGCAGCTGGACCTGGC

GGCACTGATCGTGTACTGGGAGATGGAGGACAAGAACATCATCCAGTTCGT

TCATGGCGAAGAGGATCTCAAGGTGCAGCACAGCAGCTACAGGCAGAGGGC

CCGACTGCTGAAGGACCAGCTGAGCCTGGGCAACGCCGCACTGCAAATCAC

CGACGTGAAGCTGCAGGACGCTGGCGTGTACAGGTGTATGATAAGCTACGG

CGGAGCTGACTACAAGAGAATCACGGTTAAGGTAAACGCCCCCTACGGGGG

CAGTAGCGGAAGCTCCGGCTCAAGCCACCACCATCATCATCATCACCACGG

CGGCAGCAGCGGGAGCTCAGGTAGCAGTGGTGGGGCACCTACCTCTTCCAG

CACCAAGAAGACGCAGCTCCAGTTGGAACACCTTCTCCTTGACCTCCAGAT

GATCCTGAACGGCATCAACAACTACAAAAATCCCAAGCTGACCGCGATGCT

GACGAAGAAATTCTACATGCCAAAGAAGGCCACCGAGCTGAAACACCTGCA

GTGTCTTGAGGAGGAACTTAAGCCGCTCGAGGAGGTACTGAACCTGGCCCA

GAGTAAGAACTTCCACCTGAGGCCCAGGGACCTCATCAGCAACATCAATGT

GATCGTCCTTGAGCTTAAGGGCAGCGAGACCACCTTCATGTGCGAGTATGC

GGACGAAACGGCCACAATCGTCGAGTTTCTGAATAGGTGGATCACTTTCAG

CCAGAGCATCATCTCTACCCTGACC).

In an exemplary embodiment, the PD1 ligand is PDL2. In one particular exemplary embodiment, a chimeric peptide is provided wherein the PD1 ligand is PDL2 linked to mutIL2 and comprises the amino acid sequence set forth in

SEQ ID NO: 50

(LYIIEHGSNVTLECNFDTGSHVNLGAITASLQKVENDTSPHRERATLLEE

QLPLGKASFHIPQVQVRDEGQYQCIIIYGVAWDYKYLTLKVKASGGSSGSS

GSSHHHHHHHHGGSSGSSGSSGGAPTSSSTKKTQLQLEHLLLDLQMILNGI

NNYKNPKLTAMLTKKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFH

LRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFSQSIIS

TLT).

In a particular exemplary embodiment, the composition comprises the DNA sequence set forth in

SEQ ID NO: 49

(CTGTACATCATCGAGCACGGCAGTAACGTGACCCTGGAGTGCAACTTCGA

CACCGGCAGCCACGTGAATCTGGGCGCCATCACAGCTTCACTGCAGAAGGT

GGAGAATGACACCTCTCCCCACAGGGAGCGAGCCACCCTGCTTGAGGAACA

ACTGCCTCTCGGCAAGGCCAGCTTCCACATCCCCCAGGTGCAGGTGAGGGA

CGAGGGCCAGTACCAGTGCATAATCATCTACGGCGTGGCCTGGGACTACAA

GTACCTGACACTTAAGGTGAAAGCCTCCGGCGGTTCTTCCGGCTCTTCAGG

CAGCTCACACCATCATCATCATCACCACCATGGCGGCAGCAGCGGGAGCTC

TGGTAGCAGTGGCGGTGCCCCCACCAGCAGTAGCACTAAGAAGACCCAGCT

GCAACTGGAGCACTTGCTCCTGGACCTGCAAATGATCCTCAACGGCATCAA

CAACTATAAGAACCCCAAGCTGACGGCCATGCTGACCAAAAAGTTCTACAT

GCCCAAGAAGGCCACCGAGTTGAAACACTTGCAGTGCCTGGAGGAGGAGCT

GAAGCCCCTGGAAGAGGTGCTGAACCTGGCCCAGAGCAAGAATTTTCATCT

GAGGCCTAGGGACCTGATTAGCAACATCAACGTGATCGTGTTGGAGCTTAA

AGGCTCCGAGACCACCTTTATGTGCGAGTACGCCGACGAGACCGCGACTAT

CGTGGAGTTCCTGAACAGGTGGATCACCTTTTCACAGAGCATCATAAGCAC

ACTGACC).

(h) Pharmaceutical Compositions

The present disclosure also provides pharmaceutical compositions. The pharmaceutical composition can include a composition of the invention which is detailed above, as an active ingredient and at least one pharmaceutically acceptable excipient. The pharmaceutical compositions provided herein can also include a combination therapy as described herein. In some embodiments, the combination therapy comprises a PD-1 inhibitor. In other embodiments, the combination therapy comprises a PD-L1 inhibitor.

The pharmaceutically acceptable excipient may be a diluent, a binder, a filler, a buffering agent, a pH modifying agent, a disintegrant, a dispersant, a preservative, a lubricant, taste-masking agent, a flavoring agent, or a coloring agent. The amount and types of excipients utilized to form pharmaceutical compositions may be selected according to known principles of pharmaceutical science.

In one embodiment, the excipient may be a diluent. The diluent may be compressible (i.e., plastically deformable) or abrasively brittle. Non-limiting examples of suitable compressible diluents include microcrystalline cellulose (MCC), cellulose derivatives, cellulose powder, cellulose esters (i.e., acetate and butyrate mixed esters), ethyl cellulose, methyl cellulose, hydroxypropyl cellulose, hydroxypropyl methylcellulose, sodium carboxymethylcellulose, corn starch, phosphated corn starch, pregelatinized corn starch, rice starch, potato starch, tapioca starch, starch-lactose, starch-calcium carbonate, sodium starch glycolate, glucose, fructose, lactose, lactose monohydrate, sucrose, xylose, lactitol, mannitol, malitol, sorbitol, xylitol, maltodextrin, and trehalose. Non-limiting examples of suitable abrasively brittle diluents include dibasic calcium phosphate (anhydrous or dihydrate), calcium phosphate tribasic, calcium carbonate, and magnesium carbonate.

In another embodiment, the excipient may be a binder. Suitable binders include, but are not limited to, starches, pregelatinized starches, gelatin, polyvinylpyrrolidone, cellulose, methylcellulose, sodium carboxymethylcellulose, ethylcellulose, polyacrylam ides, polyvinyloxoazolidone, polyvinylalcohols, C₁₂-C₁₈ fatty acid alcohol, polyethylene glycol, polyols, saccharides, oligosaccharides, polypeptides, oligopeptides, and combinations thereof.

In another embodiment, the excipient may be a filler. Suitable fillers include, but are not limited to, carbohydrates, inorganic compounds, and polyvinylpyrrolidone. By way of non-limiting example, the filler may be calcium sulfate, both di- and tri-basic, starch, calcium carbonate, magnesium carbonate, microcrystalline cellulose, dibasic calcium phosphate, magnesium carbonate, magnesium oxide, calcium silicate, talc, modified starches, lactose, sucrose, mannitol, or sorbitol.

In still another embodiment, the excipient may be a buffering agent. Representative examples of suitable buffering agents include, but are not limited to, phosphates, carbonates, citrates, tris buffers, and buffered saline salts (e.g., Tris buffered saline or phosphate buffered saline).

In various embodiments, the excipient may be a pH modifier. By way of non-limiting example, the pH modifying agent may be sodium carbonate, sodium bicarbonate, sodium citrate, citric acid, or phosphoric acid.

In a further embodiment, the excipient may be a disintegrant. The disintegrant may be non-effervescent or effervescent. Suitable examples of non-effervescent disintegrants include, but are not limited to, starches such as corn starch, potato starch, pregelatinized and modified starches thereof, sweeteners, clays, such as bentonite, micro-crystalline cellulose, alginates, sodium starch glycolate, gums such as agar, guar, locust bean, karaya, pecitin, and tragacanth. Non-limiting examples of suitable effervescent disintegrants include sodium bicarbonate in combination with citric acid and sodium bicarbonate in combination with tartaric acid.

In yet another embodiment, the excipient may be a dispersant or dispersing enhancing agent. Suitable dispersants may include, but are not limited to, starch, alginic acid, polyvinylpyrrolidones, guar gum, kaolin, bentonite, purified wood cellulose, sodium starch glycolate, isoamorphous silicate, and microcrystalline cellulose.

In another alternate embodiment, the excipient may be a preservative. Non-limiting examples of suitable preservatives include antioxidants, such as BHA, BHT, vitamin A, vitamin C, vitamin E, or retinyl palmitate, citric acid, sodium citrate; chelators such as EDTA or EGTA; and antimicrobials, such as parabens, chlorobutanol, or phenol.

In a further embodiment, the excipient may be a lubricant. Non-limiting examples of suitable lubricants include minerals such as talc or silica; and fats such as vegetable stearin, magnesium stearate or stearic acid.

In yet another embodiment, the excipient may be a taste-masking agent. Taste-masking materials include cellulose ethers; polyethylene glycols; polyvinyl alcohol; polyvinyl alcohol and polyethylene glycol copolymers; monoglycerides or triglycerides; acrylic polymers; mixtures of acrylic polymers with cellulose ethers; cellulose acetate phthalate; and combinations thereof.

In an alternate embodiment, the excipient may be a flavoring agent. Flavoring agents may be chosen from synthetic flavor oils and flavoring aromatics and/or natural oils, extracts from plants, leaves, flowers, fruits, and combinations thereof.

In still a further embodiment, the excipient may be a coloring agent. Suitable color additives include, but are not limited to, food, drug and cosmetic colors (FD&C), drug and cosmetic colors (D&C), or external drug and cosmetic colors (Ext. D&C).

The weight fraction of the excipient or combination of excipients in the composition may be about 99% or less, about 97% or less, about 95% or less, about 90% or less, about 85% or less, about 80% or less, about 75% or less, about 70% or less, about 65% or less, about 60% or less, about 55% or less, about 50% or less, about 45% or less, about 40% or less, about 35% or less, about 30% or less, about 25% or less, about 20% or less, about 15% or less, about 10% or less, about 5% or less, about 2%, or about 1% or less of the total weight of the composition.

The composition can be formulated into various dosage forms and administered by a number of different means that will deliver a therapeutically effective amount of the active ingredient. Such compositions can be administered orally, parenterally, or topically in dosage unit formulations containing conventional nontoxic pharmaceutically acceptable carriers, adjuvants, and vehicles as desired. Topical administration may also involve the use of transdermal administration such as transdermal patches or iontophoresis devices. The term parenteral as used herein includes subcutaneous, intravenous, intramuscular, or intrasternal injection, or infusion techniques. Formulation of drugs is discussed in, for example, Gennaro, A. R., Remington's Pharmaceutical Sciences, Mack Publishing Co., Easton, Pa. (18^th ed, 1995), and Liberman, H. A. and Lachman, L., Eds., Pharmaceutical Dosage Forms, Marcel Dekker Inc., New York, N.Y. (1980).

Solid dosage forms for oral administration include capsules, tablets, caplets, pills, powders, pellets, and granules. In such solid dosage forms, the active ingredient is ordinarily combined with one or more pharmaceutically acceptable excipients, examples of which are detailed above. Oral preparations may also be administered as aqueous suspensions, elixirs, or syrups. For these, the active ingredient may be combined with various sweetening or flavoring agents, coloring agents, and, if so desired, emulsifying and/or suspending agents, as well as diluents such as water, ethanol, glycerin, and combinations thereof.

For parenteral administration (including subcutaneous, intradermal, intravenous, intramuscular, and intraperitoneal), the preparation may be an aqueous or an oil-based solution. Aqueous solutions may include a sterile diluent such as water, saline solution, a pharmaceutically acceptable polyol such as glycerol, propylene glycol, or other synthetic solvents; an antibacterial and/or antifungal agent such as benzyl alcohol, methyl paraben, chlorobutanol, phenol, thimerosal, and the like; an antioxidant such as ascorbic acid or sodium bisulfite; a chelating agent such as etheylenediaminetetraacetic acid; a buffer such as acetate, citrate, or phosphate; and/or an agent for the adjustment of tonicity such as sodium chloride, dextrose, or a polyalcohol such as mannitol or sorbitol. The pH of the aqueous solution may be adjusted with acids or bases such as hydrochloric acid or sodium hydroxide. Oil-based solutions or suspensions may further comprise sesame, peanut, olive oil, or mineral oil.

For topical (e.g., transdermal or transmucosal) administration, penetrants appropriate to the barrier to be permeated are generally included in the preparation. Transmucosal administration may be accomplished through the use of nasal sprays, aerosol sprays, tablets, or suppositories, and transdermal administration may be via ointments, salves, gels, patches, or creams as generally known in the art.

In certain embodiments, a composition comprising a compound of the invention is encapsulated in a suitable vehicle to either aid in the delivery of the compound to target cells, to increase the stability of the composition, or to minimize potential toxicity of the composition. As will be appreciated by a skilled artisan, a variety of vehicles are suitable for delivering a composition of the present invention. Non-limiting examples of suitable structured fluid delivery systems may include nanoparticles, liposomes, microemulsions, micelles, dendrimers and other phospholipid-containing systems. Methods of incorporating compositions into delivery vehicles are known in the art.

In one alternative embodiment, a liposome delivery vehicle may be utilized. Liposomes, depending upon the embodiment, are suitable for delivery of the compound of the invention in view of their structural and chemical properties. Generally speaking, liposomes are spherical vesicles with a phospholipid bilayer membrane. The lipid bilayer of a liposome may fuse with other bilayers (e.g., the cell membrane), thus delivering the contents of the liposome to cells. In this manner, the compound of the invention may be selectively delivered to a cell by encapsulation in a liposome that fuses with the targeted cell's membrane.

Liposomes may be comprised of a variety of different types of phospholipids having varying hydrocarbon chain lengths. Phospholipids generally comprise two fatty acids linked through glycerol phosphate to one of a variety of polar groups. Suitable phospholipids include phosphatidic acid (PA), phosphatidylserine (PS), phosphatidylinositol (PI), phosphatidylglycerol (PG), diphosphatidylglycerol (DPG), phosphatidylcholine (PC), and phosphatidylethanolamine (PE). The fatty acid chains comprising the phospholipids may range from about 6 to about 26 carbon atoms in length, and the lipid chains may be saturated or unsaturated. Suitable fatty acid chains include (common name presented in parentheses) n-dodecanoate (laurate), n-tretradecanoate (myristate), n-hexadecanoate (palmitate), n-octadecanoate (stearate), n-eicosanoate (arachidate), n-docosanoate (behenate), n-tetracosanoate (lignocerate), cis-9-hexadecenoate (palmitoleate), cis-9-octadecanoate (oleate), cis,cis-9,12-octadecandienoate (linoleate), all cis-9, 12, 15-octadecatrienoate (linolenate), and all cis-5,8,11,14-eicosatetraenoate (arachidonate). The two fatty acid chains of a phospholipid may be identical or different. Acceptable phospholipids include dioleoyl PS, dioleoyl PC, distearoyl PS, distearoyl PC, dimyristoyl PS, dimyristoyl PC, dipalmitoyl PG, stearoyl, oleoyl PS, palmitoyl, linolenyl PS, and the like.

The phospholipids may come from any natural source, and, as such, may comprise a mixture of phospholipids. For example, egg yolk is rich in PC, PG, and PE, soy beans contains PC, PE, PI, and PA, and animal brain or spinal cord is enriched in PS. Phospholipids may come from synthetic sources too. Mixtures of phospholipids having a varied ratio of individual phospholipids may be used. Mixtures of different phospholipids may result in liposome compositions having advantageous activity or stability of activity properties. The above mentioned phospholipids may be mixed, in optimal ratios with cationic lipids, such as N-(1-(2,3-dioleolyoxy)propyl)-N,N,N-trimethyl ammonium chloride, 1,1′-dioctadecyl-3,3,3′,3′-tetramethylindocarbocyanine perchloarate, 3,3′-deheptyloxacarbocyanine iodide, 1,1′-dedodecyl-3,3,3′,3′-tetramethylindocarbocyanine perchloarate, 1,1′-dioleyl-3,3,3′,3′-tetramethylindo carbocyanine methanesulfonate, N-4-(delinoleylaminostyryl)-N-methylpyridinium iodide, or 1,1,-dilinoleyl-3,3,3′,3′-tetramethylindocarbocyanine perchloarate.

Liposomes may optionally comprise sphingolipids, in which spingosine is the structural counterpart of glycerol and one of the one fatty acids of a phosphoglyceride, or cholesterol, a major component of animal cell membranes. Liposomes may optionally, contain pegylated lipids, which are lipids covalently linked to polymers of polyethylene glycol (PEG). PEGs may range in size from about 500 to about 10,000 daltons.

Liposomes may further comprise a suitable solvent. The solvent may be an organic solvent or an inorganic solvent. Suitable solvents include, but are not limited to, dimethylsulfoxide (DMSO), methylpyrrolidone, N-methylpyrrolidone, acetronitrile, alcohols, dimethylformamide, tetrahydrofuran, or combinations thereof.

Liposomes carrying the compound of the invention (i.e., having at least one methionine compound) may be prepared by any known method of preparing liposomes for drug delivery, such as, for example, detailed in U.S. Pat. Nos. 4,241,046, 4,394,448, 4,529,561, 4,755,388, 4,828,837, 4,925,661, 4,954,345, 4,957,735, 5,043,164, 5,064,655, 5,077,211 and 5,264,618, the disclosures of which are hereby incorporated by reference in their entirety. For example, liposomes may be prepared by sonicating lipids in an aqueous solution, solvent injection, lipid hydration, reverse evaporation, or freeze drying by repeated freezing and thawing. In a preferred embodiment the liposomes are formed by sonication. The liposomes may be multilamellar, which have many layers like an onion, or unilamellar. The liposomes may be large or small. Continued high-shear sonication tends to form smaller unilamellar liposomes.

As would be apparent to one of ordinary skill, all of the parameters that govern liposome formation may be varied. These parameters include, but are not limited to, temperature, pH, concentration of methionine compound, concentration and composition of lipid, concentration of multivalent cations, rate of mixing, presence of and concentration of solvent.

In another embodiment, a composition of the invention may be delivered to a cell as a microemulsion. Microemulsions are generally clear, thermodynamically stable solutions comprising an aqueous solution, a surfactant, and “oil.” The “oil” in this case, is the supercritical fluid phase. The surfactant rests at the oil-water interface. Any of a variety of surfactants are suitable for use in microemulsion formulations including those described herein or otherwise known in the art. The aqueous microdomains suitable for use in the invention generally will have characteristic structural dimensions from about 5 nm to about 100 nm. Aggregates of this size are poor scatterers of visible light and hence, these solutions are optically clear. As will be appreciated by a skilled artisan, microemulsions can and will have a multitude of different microscopic structures including sphere, rod, or disc shaped aggregates. In one embodiment, the structure may be micelles, which are the simplest microemulsion structures that are generally spherical or cylindrical objects. Micelles are like drops of oil in water, and reverse micelles are like drops of water in oil. In an alternative embodiment, the microemulsion structure is the lamellae. It comprises consecutive layers of water and oil separated by layers of surfactant. The “oil” of microemulsions optimally comprises phospholipids. Any of the phospholipids detailed above for liposomes are suitable for embodiments directed to microemulsions. The composition of the invention may be encapsulated in a microemulsion by any method generally known in the art.

In yet another embodiment, a composition of the invention may be delivered in a dendritic macromolecule, or a dendrimer. Generally speaking, a dendrimer is a branched tree-like molecule, in which each branch is an interlinked chain of molecules that divides into two new branches (molecules) after a certain length. This branching continues until the branches (molecules) become so densely packed that the canopy forms a globe. Generally, the properties of dendrimers are determined by the functional groups at their surface. For example, hydrophilic end groups, such as carboxyl groups, would typically make a water-soluble dendrimer. Alternatively, phospholipids may be incorporated in the surface of a dendrimer to facilitate absorption across the skin. Any of the phospholipids detailed for use in liposome embodiments are suitable for use in dendrimer embodiments. Any method generally known in the art may be utilized to make dendrimers and to encapsulate compositions of the invention therein. For example, dendrimers may be produced by an iterative sequence of reaction steps, in which each additional iteration leads to a higher order dendrimer. Consequently, they have a regular, highly branched 3D structure, with nearly uniform size and shape. Furthermore, the final size of a dendrimer is typically controlled by the number of iterative steps used during synthesis. A variety of dendrimer sizes are suitable for use in the invention. Generally, the size of dendrimers may range from about 1 nm to about 100 nm

II. Methods

In an aspect, the invention encompasses a method to deliver a cytokine to a target cell. The method comprises contacting a target cell with a composition comprising a cytokine linked to a ligand, wherein the ligand specifically binds to a receptor on the target cell. Additionally, the method comprises contacting a target cell with a composition comprising a chimeric peptide as described in Section I. A target cell may be any cell comprising a target receptor for which the ligand specifically binds to. The ligand and specific binding are described in Section I. In certain embodiments, a target cell may be an immune cell. Non-limiting example of immune cells include macrophages, B lymphocytes, T lymphocytes, mast cells, monocytes, dendritic cells, eosinophils, natural killer cells, basophils, neutrophils. In certain embodiments, an immune cell is selected from the group consisting of a macrophage, B lymphocyte, T lymphocyte, mast cell, monocyte, dendritic cell, eosinophil, natural killer cell, basophil, and neutrophil. In a specific embodiment, a target cell is a natural killer (NK) cell and/or a CD8+ T cell. In other embodiments, a target cell is a NKG2D-expressing cell. Non-limiting examples of NKG2D-expressing cell include natural killer (NK) cells and CD8+ T cells (both αβ and γδ). In still other embodiments, a target cell is a PD1-expressing cell. Non-limiting examples of PD1-expressing cells include NK cells, CD8+ T cells, and myeloid cells. In some embodiments, the method of therapy comprises a chimeric peptide comprising a PD1 ligand and a cytokine. In another embodiment, the chimeric peptide further comprises a linker. In one embodiment, the PD1 ligand is PDL1. In another embodiment, the PD1 ligand is PDL2. In still another embodiment, the PD1 ligand is an antibody specific to PD1. In another embodiment, the cytokine is IL2. In some embodiments, the IL2 is a mutant R38A/F42K form of IL2. In some embodiments, the method further comprises administering a combination therapy as provided herein. In some embodiments, the combination therapy comprises a PD-1 inhibitor. In other embodiments, the PD-1 inhibitor is an anti-PD-1 antibody. In some embodiments, the combination therapy comprises a PD-L1 inhibitor. In other embodiments, the PD-L1 inhibitor is an anti-PD-L1 antibody. In one embodiment, provided herein is a method to deliver a cytokine to a target cell comprising administration of a composition provided herein. In one embodiment, provided herein is a method to deliver a cytokine to a target cell comprising administration of a combination therapy provided herein. In some embodiments, the combination therapy includes a PD-1 inhibitor provided herein and a chimeric peptide that includes a cytokine peptide and an anti-NKG2D antibody. In certain embodiments, the cytokine peptide is a cytokine as described hereinabove. In some embodiments, the anti-NKG2D antibody is as described hereinabove. In one embodiment, the combination therapy comprises an OMCP-IL2 fusion protein and a PD-1 inhibitor. In another embodiment, the combination therapy comprises an OMCP-IL2 fusion protein and an anti-PD-1 antibody. In some embodiments, the fusion protein further comprises a linker. In one embodiment, the combination therapy comprises an OMCP-IL2 chimeric protein and a PD-1 inhibitor. In another embodiment, the combination therapy comprises an OMCP-IL2 chimeric protein and an anti-PD-1 antibody. In some embodiments, the chimeric protein further comprises a linker. In other embodiments, the combination therapy comprises an anti-NKG2D antibody, IL2 and a PD1 inhibitor. In some embodiments, the combination therapy comprises an anti-NKG2D antibody, IL2 and an anti-PD1 antibody. In some embodiment, the anti-PD-1 antibody is an antagonistic antibody. In certain embodiments, the anti-NKG2D antibody is KYK-1. In other embodiments, the anti-NKG2D antibody is KYK-2. In some embodiments, the anti-NKG2D antibody and the IL2 are provided as a chimeric polypeptide. In some embodiments, the chimeric polypeptide further comprises a linker. In some embodiments, the anti-NKG2D antibody and the IL2 are provided as a fusion protein. In some embodiments, the fusion protein further comprises a linker. In some embodiments, the combination therapy comprises an anti-NKG2D scFv, IL2 and a PD1 inhibitor. In some embodiments, the combination therapy comprises an anti-NKG2D scFv, IL2 and an anti-PD1 antibody. In some embodiment, the anti-PD-1 antibody is an antagonistic antibody. In certain embodiments, the anti-NKG2D scFv is a KYK-1 scFv. In other embodiments, the anti-NKG2D scFv is a KYK-2 scFv. In some embodiments, the anti-NKG2D scFv and the IL2 are provided as a chimeric polypeptide. In some embodiments, the chimeric polypeptide further comprises a linker. In some embodiments, the anti-NKG2D scFv and the IL2 are provided as a fusion protein. In some embodiments, the fusion protein further comprises a linker. In some embodiments, the IL2 is a mutant R38A/F42K form of IL2. In some embodiments, the target cell is a target cell of a subject. In certain embodiments, the subject is in need thereof. In certain embodiments, the subject is administered an effective amount of the combination therapy. The term “effective amount” as used herein refers to the amount of a pharmaceutical composition provided herein which is sufficient to result in the desired outcome. In specific embodiments, the subject is a human. In certain embodiments, the subject is a subject having a cancer or tumor. In specific embodiments, the cancer or tumor is a lung cancer or tumor.

In another aspect, the invention encompasses a method to activate immune cells. The method comprises contacting an immune cell with a composition comprising a cytokine linked to a ligand, wherein the ligand specifically binds to a receptor on the immune cell thereby activating the cell. Additionally, in some embodiments, the method comprises contacting an immune cell with a composition comprising a chimeric peptide as described in Section I. Non-limiting example of immune cells include macrophages, B lymphocytes, T lymphocytes, mast cells, monocytes, dendritic cells, eosinophils, natural killer cells, basophils, neutrophils. In certain embodiments, an immune cell is selected from the group consisting of a macrophage, B lymphocyte, T lymphocyte, mast cell, monocyte, dendritic cell, eosinophil, natural killer cell, basophil, and neutrophil. In a specific embodiment, an immune cell is a natural killer (NK) cell and/or a CD8⁺ T cell. In still other embodiments, a target cell is a PD1-expressing cell. Non-limiting examples of PD1-expressing cells include NK cells, CD8⁺ T cells, and myeloid cells. To facilitate activation of immune cells, a cytokine may be a proinflammatory cytokine. The term “proinflammatory cytokine” is a cytokine which promotes systemic inflammation. A skilled artisan would be able to determine those cytokines that are proinflammatory. In certain embodiments, a proinflammatory cytokine is IL1α, IL1β, IL2, IL3, IL6, IL7, IL9, IL12, IL15, IL17, IL18, IL21, IFNα, IFNγ, TNFα, MIF, G-CSF, GM-CSF, TNFalpha, CD40L, 4-1BBL, OX40L, RANKL, or mutants thereof. In an embodiment, a proinflammatory cytokine is an IL1 family cytokine. In certain embodiments, an IL1 family cytokine is selected from the group consisting of IL1α, IL1β, IL1Ra, IL18, IL36Ra, IL36α, IL37, IL36β, IL36γ, IL38, IL33 and mutants thereof. In a specific embodiment, a proinflammatory cytokine is selected from the group consisting of IL2, IL7, IL15, IL18, IL21 and mutants thereof. In another specific embodiment, a proinflammatory cytokine is selected from the group consisting of IL2, IL15, IL18, and mutants thereof. In an exemplary embodiment, a proinflammatory cytokine is IL2 or a mutant thereof. In other certain embodiments, a proinflammatory cytokine is a TNFSF family cytokine. In certain embodiments, the TNFSF family cytokine is selected from a group containing TNFalpha, CD40L, 4-1BBL, OX40L, or RANKL. In another specific embodiment, the proinflammatory cytokine is selected from either OX40L or 4-1BBL. In an exemplary embodiment, a proinflammatory cytokine is OX40L or a mutant thereof. In another exemplary embodiment, a proinflammatory cytokine is 4-1BBL or a mutant thereof. Activation of the immune cells may result in lysis of tumor cells. Accordingly, activation of immune cells may be measured by determining the amount of tumor cell lysis. In an embodiment, activation of the immune cells may result in about 10% to about 100% lysis of tumor cells. In another embodiment, activation of the immune cells may result in about 20% to about 80% lysis of tumor cells. In still another embodiment, activation of the immune cells may result in greater than 40% lysis of tumor cells. For example, activation of the immune cells may result in greater than 40%, greater than 45%, greater than 50%, greater than 55%, greater than 60%, greater than 65%, greater than 70%, greater than 75%, greater than 80%, greater than 85%, greater than 90%, greater than 95%, or greater than 99% lysis of tumor cells. The lysis of tumor cells may be measured using any standard assay (e.g., caspase assays, TUNEL and DNA fragmentation assays, cell permeability assays, and Annexin V assays). In some embodiments, the method of therapy comprises a chimeric peptide comprising a PD1 ligand and a cytokine. In another embodiment, the chimeric peptide further comprises a linker. In one embodiment, the PD1 ligand is PDL1. In another embodiment, the PD1 ligand is PDL2. In still another embodiment, the PD1 ligand is an antibody specific to PD1. In another embodiment, the cytokine is IL2. In some embodiments, the IL2 is a mutant R38A/F42K form of IL2. In some embodiments, the method further comprises administering a combination therapy as provided herein. In some embodiments, the combination therapy comprises a PD-1 inhibitor. In other embodiments, the PD-1 inhibitor is an anti-PD-1 antibody. In some embodiments, the combination therapy comprises a PD-L1 inhibitor. In other embodiments, the PD-L1 inhibitor is an anti-PD-L1 antibody. In one embodiment, provided herein is a method to activate immune cells, comprising administration of a composition provided herein. In one embodiment, provided herein is a method to activate immune cells, comprising administration of a combination therapy provided herein. In some embodiments, the combination therapy includes a PD-1 inhibitor provided herein and a chimeric peptide that includes a cytokine peptide and an anti-NKG2D antibody. In certain embodiments, the cytokine peptide is a cytokine as described hereinabove. In some embodiments, the anti-NKG2D antibody is as described hereinabove. In one embodiment, the combination therapy comprises an OMCP-IL2 fusion protein and a PD-1 inhibitor. In another embodiment, the combination therapy comprises an OMCP-IL2 fusion protein and an anti-PD-1 antibody. In some embodiments, the fusion protein further comprises a linker. In one embodiment, the combination therapy comprises an OMCP-IL2 chimeric protein and a PD-1 inhibitor. In another embodiment, the combination therapy comprises an OMCP-IL2 chimeric protein and an anti-PD-1 antibody. In some embodiments, the chimeric protein further comprises a linker. In other embodiments, the combination therapy comprises an anti-NKG2D antibody, IL2 and a PD1 inhibitor. In some embodiments, the combination therapy comprises an anti-NKG2D antibody, IL2 and an anti-PD1 antibody. In some embodiment, the anti-PD-1 antibody is an antagonistic antibody. In certain embodiments, the anti-NKG2D antibody is KYK-1. In other embodiments, the anti-NKG2D antibody is KYK-2. In some embodiments, the anti-NKG2D antibody and the IL2 are provided as a chimeric polypeptide. In some embodiments, the chimeric polypeptide further comprises a linker. In some embodiments, the anti-NKG2D antibody and the IL2 are provided as a fusion protein. In some embodiments, the fusion protein further comprises a linker. In some embodiments, the combination therapy comprises an anti-NKG2D scFv, IL2 and a PD1 inhibitor. In some embodiments, the combination therapy comprises an anti-NKG2D scFv, IL2 and an anti-PD1 antibody. In some embodiment, the anti-PD-1 antibody is an antagonistic antibody. In certain embodiments, the anti-NKG2D scFv is a KYK-1 scFv. In other embodiments, the anti-NKG2D scFv is a KYK-2 scFv. In some embodiments, the anti-NKG2D scFv and the IL2 are provided as a chimeric polypeptide. In some embodiments, the chimeric polypeptide further comprises a linker. In some embodiments, the anti-NKG2D scFv and the IL2 are provided as a fusion protein. In some embodiments, the fusion protein further comprises a linker. In some embodiments, the IL2 is a mutant R38A/F42K form of IL2. In some embodiments, the immune cells are immune cells of a subject. In certain embodiments, the subject is in need thereof. In certain embodiments, the subject is administered an effective amount of the combination therapy. In specific embodiments, the subject is a human. In certain embodiments, the subject is a subject having a cancer or tumor. In specific embodiments, the cancer or tumor is a lung cancer or tumor.

In still another aspect, the invention encompasses a method to treat a tumor. The method comprises identifying a subject with a tumor and administering to the subject a composition comprising a cytokine linked to a ligand, wherein the ligand specifically binds to a receptor on a target cell. Additionally, the method comprises administering to the subject a composition comprising a chimeric peptide as described in Section I. Specifically, the inventors have shown that delivering a cytokine to a target cell activates the cells bound by the composition, wherein the activated cells specifically lyse tumor cells thereby reducing the amount of cancer cells. In a specific embodiment, a cytokine is a proinflammatory cytokine as described in the preceding paragraph. Accordingly, a composition of the present invention, may be used in treating, stabilizing and preventing cancer and associated diseases in a subject. By “treating, stabilizing, or preventing cancer” is meant causing a reduction in the size of a tumor or in the number of cancer cells, slowing or preventing an increase in the size of a tumor or cancer cell proliferation, increasing the disease-free survival time between the disappearance of a tumor or other cancer and its reappearance, preventing an initial or subsequent occurrence of a tumor or other cancer, or reducing an adverse symptom associated with a tumor or other cancer. The inventors have shown that a composition of the invention activates natural killer (NK) cells bound by the composition, wherein the activated NK cells specifically lyse tumor cells thereby reducing the amount of tumor cells. For example, as cancerous cells are “stressed”, NKG2D ligands become upregulated, rendering the cell susceptible to NK cell-mediated lysis. In a desired embodiment, the percent of tumor or cancerous cells surviving the treatment is at least 20, 30, 40, 50, 60, 70, 80, 90 or 100% lower than the initial number of tumor or cancerous cells, as measured using any standard assay (e.g., caspase assays, TUNEL and DNA fragmentation assays, cell permeability assays, and Annexin V assays). Desirably, the decrease in the number of tumor or cancerous cells induced by administration of a composition of the invention is at least 2, 5, 10, 15, 20, 25, 30, 35, 40, 45 or 50-fold greater than the decrease in the number of non-tumor or non-cancerous cells. Desirably, the methods of the present invention result in a decrease of 20, 30, 40, 50, 60, 50, 80, 90 or 100% in the size of a tumor or in the number of cancerous cells, as determined using standard methods. Desirably, at least 20, 30, 40, 50, 60, 70, 80, 90, or 95% of the treated subjects have a complete remission in which all evidence of the tumor or cancer disappears. Desirably, the tumor or cancer does not reappear or reappears after at least 1, 2, 3, 4, 5, 10, 15, or 20 years. In some embodiments, the method further comprises administering a chimeric peptide comprising a PD1 ligand and a cytokine. In another embodiment, the chimeric peptide further comprises a linker. In one embodiment, the PD1 ligand is PDL1. In another embodiment, the PD1 ligand is PDL2. In still another embodiment, the PD1 ligand is an antibody specific to PD1. In another embodiment, the cytokine is IL2. In some embodiments, the IL2 is a mutant R38A/F42K form of IL2. In some embodiments, the method further comprises administering a combination therapy as provided herein. In some embodiments, the combination therapy comprises a PD-1 inhibitor. In other embodiments, the PD-1 inhibitor is an anti-PD-1 antibody. In some embodiments, the combination therapy comprises a PD-L1 inhibitor. In other embodiments, the PD-L1 inhibitor is an anti-PD-L1 antibody. In one embodiment, provided herein is a method to treat a tumor in a subject, comprising administering to the subject a composition provided herein. In one embodiment, provided herein is a method to treat a tumor in a subject, comprising administering to the subject a combination therapy provided herein. In some embodiments, the combination therapy includes a PD-1 inhibitor provided herein and a chimeric peptide that includes a cytokine peptide and an anti-NKG2D antibody. In certain embodiments, the cytokine peptide is a cytokine as described hereinabove. In some embodiments, the anti-NKG2D antibody is as described hereinabove. In one embodiment, the combination therapy comprises an OMCP-IL2 fusion protein and a PD-1 inhibitor. In another embodiment, the combination therapy comprises an OMCP-IL2 fusion protein and an anti-PD-1 antibody. In some embodiments, the fusion protein further comprises a linker. In one embodiment, the combination therapy comprises an OMCP-IL2 chimeric protein and a PD-1 inhibitor. In another embodiment, the combination therapy comprises an OMCP-IL2 chimeric protein and an anti-PD-1 antibody. In some embodiments, the chimeric protein further comprises a linker. In other embodiments, the combination therapy comprises an anti-NKG2D antibody, IL2 and a PD1 inhibitor. In some embodiments, the combination therapy comprises an anti-NKG2D antibody, IL2 and an anti-PD1 antibody. In some embodiment, the anti-PD-1 antibody is an antagonistic antibody. In certain embodiments, the anti-NKG2D antibody is KYK-1. In other embodiments, the anti-NKG2D antibody is KYK-2. In some embodiments, the anti-NKG2D antibody and the IL2 are provided as a chimeric polypeptide. In some embodiments, the chimeric polypeptide further comprises a linker. In some embodiments, the anti-NKG2D antibody and the IL2 are provided as a fusion protein. In some embodiments, the fusion protein further comprises a linker. In some embodiments, the combination therapy comprises an anti-NKG2D scFv, IL2 and a PD1 inhibitor. In some embodiments, the combination therapy comprises an anti-NKG2D scFv, IL2 and an anti-PD1 antibody. In some embodiment, the anti-PD-1 antibody is an antagonistic antibody. In certain embodiments, the anti-NKG2D scFv is a KYK-1 scFv. In other embodiments, the anti-NKG2D scFv is a KYK-2 scFv. In some embodiments, the anti-NKG2D scFv and the IL2 are provided as a chimeric polypeptide. In some embodiments, the chimeric polypeptide further comprises a linker. In some embodiments, the anti-NKG2D scFv and the IL2 are provided as a fusion protein. In some embodiments, the fusion protein further comprises a linker. In some embodiments, the IL2 is a mutant R38A/F42K form of IL2. In certain embodiments, the subject is in need thereof. In certain embodiments, the subject is administered an effective amount of the combination therapy. In specific embodiments, the subject is a human. In specific embodiments, the tumor is a lung tumor.

In another aspect, the invention encompasses a method to suppress immune cells. The method comprises contacting an immune cell with a composition comprising a cytokine linked to a ligand, wherein the ligand specifically binds to a receptor on the immune cell thereby suppressing the cell. Additionally, the method comprises contacting an immune cells with a composition comprising a chimeric peptide as described in Section I. Non-limiting example of immune cells include macrophages, B lymphocytes, T lymphocytes, mast cells, monocytes, dendritic cells, eosinophils, natural killer cells, basophils, neutrophils. In certain embodiments, an immune cell is selected from the group consisting of a macrophage, B lymphocyte, T lymphocyte, mast cell, monocyte, dendritic cell, eosinophil, natural killer cell, basophil, and neutrophil. In a specific embodiment, an immune cell is a natural killer (NK) cell and/or a CD8+ T cell. In a specific embodiment, the immune cell expresses NKG2D. In an alternate specific embodiment, the immune cell expresses PD1. To facilitate suppression of immune cells, a cytokine may be an anti-inflammatory cytokine. The term “anti-inflammatory cytokine” is a cytokine that counteracts various aspects of inflammation, for example cell activation or the production of proinflammatory cytokines, and thus contributes to the control of the magnitude of the inflammatory response. A skilled artisan would be able to determine those cytokines that are anti-inflammatory. In certain embodiments, an anti-inflammatory cytokine is IL4, IL5, IL10, IL11, IL13, IL16, IL35, IFNα, TGFβ, G-CSF or a mutant thereof. In a specific embodiment, an anti-inflammatory cytokine is IL10 or a mutant thereof. In another embodiment, the invention encompasses a method to kill immune cells. The method comprises contacting an immune cell with a composition comprising a toxin linked to a ligand, wherein the ligand specifically binds to a receptor on the immune cell thereby killing the cell. Suppression or killing of the immune cells may result in treatment, stabilization and prevention of autoimmune diseases caused by overactive immune cells. NKG2D-expressing cells and/or aberrant expression of host NKG2DLs have been implicated in diabetes, celiac disease and rheumatoid arthritis. For example, NK cells can recognize pancreatic beta cells and destroy them. The destruction of pancreatic beta cells may lead to type 1 diabetes. By way of another example, overactive immune cells are involved in transplant/graft rejection. Accordingly, a composition of the present invention, may be used in treating, stabilizing and preventing an autoimmune disease in a subject. In a specific embodiment, the autoimmune disease is type 1 diabetes. In another specific embodiment, the autoimmune disease is transplant or graft rejection. In still another specific embodiment, the autoimmune disease is rheumatoid arthritis. In some embodiments, the method further comprises administering a combination therapy as provided herein. In some embodiments, the combination therapy comprises a PD-1 inhibitor. In other embodiments, the PD-1 inhibitor is an anti-PD-1 antibody. In some embodiments, the combination therapy comprises a PD-L1 inhibitor. In other embodiments, the PD-L1 inhibitor is an anti-PD-L1 antibody. In one embodiment, provided herein is a method to suppress immune cells in a subject, comprising administering to the subject a composition provided herein. In one embodiment, provided herein is a method to suppress immune cells in a subject, comprising administering to the subject a combination therapy provided herein. In some embodiments, the combination therapy includes a PD-1 inhibitor provided herein and a chimeric peptide that includes a cytokine peptide and an anti-NKG2D antibody. In certain embodiments, the cytokine peptide is a cytokine as described hereinabove. In some embodiments, the anti-NKG2D antibody is as described hereinabove. In some embodiments, the chimeric protein further comprises a linker. In some embodiment, the anti-PD-1 antibody is an antagonistic antibody. In certain embodiments, the anti-NKG2D antibody is KYK-1. In other embodiments, the anti-NKG2D antibody is KYK-2. In certain embodiments, the subject is in need thereof. In certain embodiments, the subject is administered an effective amount of the combination therapy. In specific embodiments, the subject is a human. In certain embodiments, the subject is a subject having a cancer or tumor. In specific embodiments, the cancer or tumor is a lung cancer or tumor.

In still yet another aspect, the invention encompasses a method to treat an infection comprising administering a composition comprising a cytokine linked to a ligand. For example, a composition comprising a cytokine linked to a ligand may specifically bind an immune cell that is then activated to target and lyse the infected host cell. Additionally, the method comprises administering to the subject a composition comprising a chimeric peptide as described in Section I. The term “infection” as used herein includes the presence of pathogens in or on a subject, which, if its growth were inhibited, would result in a benefit to the subject. As such, the term “infection” in addition to referring to the presence of pathogens also refers to normal flora which are not desirable. The term “pathogen” as used herein refers to an infectious agent that can produce disease. Non-limiting examples of an infectious agent include virus, bacterium, prion, fungus, viroid, or parasite that cause disease in a subject. In a specific embodiment, an infection is caused by pathogens such as bacteria or viruses. In certain embodiments, the infection is an intracellular infection. In an embodiment, the infection is a viral infection. In another embodiment, the viral infection is caused by a flavivirus. Flavivirus is a genus of viruses in the family Flaviviridae. Non-limiting examples of flaviviruses include Gadget's Gully virus, Kadam virus, Kyasanur Forrest disease virus, Langat virus, Omsk hemorrhagic fever virus, Tick-borne encephalitis virus, Louping ill virus, Aroa virus, Dengue viruses 1-4, Kedougou virus, Cacipacore virus, Koutango virus, Murray Valley encephalitis virus, St. Louis encephalitis virus, Usutu virus, West Nile virus, Yaounde virus, Kokobera virus group, Kokobera virus, Bagaza virus, Ilheus virus, Israel turkey meningoencephalomyelitis virus, Ntaya virus, Tembusu virus, Zika virus, Banzi virus, Bouboui virus, Edge Hill virus, Jugra virus, Saboya virus, Sepik virus, Uganda S virus, Wesselsbron virus, Yellow fever virus, Entebbe bat virus, Yokose virus, Apoi virus, Cowbone Ridge virus, Jutiapa virus, Modoc virus, Sal Vieja virus, San Perlita virus, Bukalasa bat virus, Carey Island virus, Dakar bat virus, Montana myotis leukoencephalitis virus, Phnom Penh bat virus, Rio Bravo virus, hepatitis C virus, e.g., hepatitis C virus genotypes 1-6, and GB virus A and B. In a certain embodiment, the flavivirus may be selected from the group consisting of West Nile virus, dengue virus, Japanese encephalitis virus, and yellow fever virus. In a specific embodiment, the viral infection is caused by West Nile virus. In certain embodiments, a pathogen, more specifically a virus, can induce the expression of proteins for which NKG2D binds. Accordingly, a composition comprising a cytokine linked to a ligand may specifically bind a NK cell that is then activated to target and lyse the infected host cell expressing NKG2D. In another embodiment, a composition comprising a cytokine linked to a ligand may activate cytotoxic T lymphocytes that recognize infected cells via other mechanisms for targeted killing. In some embodiments, the method further comprises administering a chimeric peptide comprising a PD1 ligand and a cytokine. In another embodiment, the chimeric peptide further comprises a linker. In one embodiment, the PD1 ligand is PDL1. In another embodiment, the PD1 ligand is PDL2. In still another embodiment, the PD1 ligand is an antibody specific to PD1. In another embodiment, the cytokine is IL2. In some embodiments, the IL2 is a mutant R38A/F42K form of IL2. In some other embodiments, the method further comprises administering a combination therapy as provided herein. In some embodiments, the combination therapy comprises a PD-1 inhibitor. In other embodiments, the PD-1 inhibitor is an anti-PD-1 antibody. In some embodiments, the combination therapy comprises a PD-L1 inhibitor. In other embodiments, the PD-L1 inhibitor is an anti-PD-L1 antibody. In one embodiment, provided herein is a method to treat an infection in a subject, comprising administering to the subject a composition provided herein. In one embodiment, provided herein is a method to treat an infection in a subject, comprising administering to the subject a combination therapy provided herein. In some embodiments, the combination therapy includes a PD-1 inhibitor provided herein and a chimeric peptide that includes a cytokine peptide and an anti-NKG2D antibody. In certain embodiments, the cytokine peptide is a cytokine as described hereinabove. In some embodiments, the anti-NKG2D antibody is as described hereinabove. In one embodiment, the combination therapy comprises an OMCP-IL2 fusion protein and a PD-1 inhibitor. In another embodiment, the combination therapy comprises an OMCP-IL2 fusion protein and an anti-PD-1 antibody. In some embodiments, the fusion protein further comprises a linker. In one embodiment, the combination therapy comprises an OMCP-IL2 chimeric protein and a PD-1 inhibitor. In another embodiment, the combination therapy comprises an OMCP-IL2 chimeric protein and an anti-PD-1 antibody. In some embodiments, the chimeric protein further comprises a linker. In other embodiments, the combination therapy comprises an anti-NKG2D antibody, IL2 and a PD1 inhibitor. In some embodiments, the combination therapy comprises an anti-NKG2D antibody, IL2 and an anti-PD1 antibody. In some embodiment, the anti-PD-1 antibody is an antagonistic antibody. In certain embodiments, the anti-NKG2D antibody is KYK-1. In other embodiments, the anti-NKG2D antibody is KYK-2. In some embodiments, the anti-NKG2D antibody and the IL2 are provided as a chimeric polypeptide. In some embodiments, the chimeric polypeptide further comprises a linker. In some embodiments, the anti-NKG2D antibody and the IL2 are provided as a fusion protein. In some embodiments, the fusion protein further comprises a linker. In some embodiments, the combination therapy comprises an anti-NKG2D scFv, IL2 and a PD1 inhibitor. In some embodiments, the combination therapy comprises an anti-NKG2D scFv, IL2 and an anti-PD1 antibody. In some embodiment, the anti-PD-1 antibody is an antagonistic antibody. In certain embodiments, the anti-NKG2D scFv is a KYK-1 scFv. In other embodiments, the anti-NKG2D scFv is a KYK-2 scFv. In some embodiments, the anti-NKG2D scFv and the IL2 are provided as a chimeric polypeptide. In some embodiments, the chimeric polypeptide further comprises a linker. In some embodiments, the anti-NKG2D scFv and the IL2 are provided as a fusion protein. In some embodiments, the fusion protein further comprises a linker. In some embodiments, the IL2 is a mutant R38A/F42K form of IL2. In certain embodiments, the subject is in need thereof. In certain embodiments, the subject is administered an effective amount of the combination therapy. In specific embodiments, the subject is a human.

In a different aspect, the invention encompasses a method to alleviate immunosuppression related to radiation exposure or lymphotoxic substances comprising administering a composition comprising a cytokine linked to a ligand. Additionally, the method comprises administering a composition comprising a chimeric peptide as described in Section I. Additionally, a composition of the invention may be used to raise CD4 counts in HIV positive subjects. For example, a composition of the invention may be used to activate immune cells which can help restore the immune system of the subject. In some embodiments, the method further comprises administering a chimeric peptide comprising a PD1 ligand and a cytokine. In another embodiment, the chimeric peptide further comprises a linker. In one embodiment, the PD1 ligand is PDL1. In another embodiment, the PD1 ligand is PDL2. In still another embodiment, the PD1 ligand is an antibody specific to PD1. In another embodiment, the cytokine is IL2. In some embodiments, the IL2 is a mutant R38A/F42K form of IL2. In some embodiments, the method further comprises administering a combination therapy as provided herein. In some embodiments, the combination therapy comprises a PD-1 inhibitor. In other embodiments, the PD-1 inhibitor is an anti-PD-1 antibody. In some embodiments, the combination therapy comprises a PD-L1 inhibitor. In other embodiments, the PD-L1 inhibitor is an anti-PD-L1 antibody. In one embodiment, provided herein is a method to alleviate immunosuppression related to radiation exposure or lymphotoxic substances in a subject, comprising administering to the subject a composition provided herein. In one embodiment, provided herein is a method to alleviate immunosuppression related to radiation exposure or lymphotoxic substances in a subject, comprising administering to the subject a combination therapy provided herein. In one embodiment, the immunosuppression is related to radiation exposure. In another embodiment, the immunosuppression is related to lympotoxic substances. In some embodiments, the combination therapy includes a PD-1 inhibitor provided herein and a chimeric peptide that includes a cytokine peptide and an anti-NKG2D antibody. In certain embodiments, the cytokine peptide is a cytokine as described hereinabove. In some embodiments, the anti-NKG2D antibody is as described hereinabove. In one embodiment, the combination therapy comprises an OMCP-IL2 fusion protein and a PD-1 inhibitor. In another embodiment, the combination therapy comprises an OMCP-IL2 fusion protein and an anti-PD-1 antibody. In some embodiments, the fusion protein further comprises a linker. In one embodiment, the combination therapy comprises an OMCP-IL2 chimeric protein and a PD-1 inhibitor. In another embodiment, the combination therapy comprises an OMCP-IL2 chimeric protein and an anti-PD-1 antibody. In some embodiments, the chimeric protein further comprises a linker. In other embodiments, the combination therapy comprises an anti-NKG2D antibody, IL2 and a PD1 inhibitor. In some embodiments, the combination therapy comprises an anti-NKG2D antibody, IL2 and an anti-PD1 antibody. In some embodiment, the anti-PD-1 antibody is an antagonistic antibody. In certain embodiments, the anti-NKG2D antibody is KYK-1. In other embodiments, the anti-NKG2D antibody is KYK-2. In some embodiments, the anti-NKG2D antibody and the IL2 are provided as a chimeric polypeptide. In some embodiments, the chimeric polypeptide further comprises a linker. In some embodiments, the anti-NKG2D antibody and the IL2 are provided as a fusion protein. In some embodiments, the fusion protein further comprises a linker. In some embodiments, the combination therapy comprises an anti-NKG2D scFv, IL2 and a PD1 inhibitor. In some embodiments, the combination therapy comprises an anti-NKG2D scFv, IL2 and an anti-PD1 antibody. In some embodiment, the anti-PD-1 antibody is an antagonistic antibody. In certain embodiments, the anti-NKG2D scFv is a KYK-1 scFv. In other embodiments, the anti-NKG2D scFv is a KYK-2 scFv. In some embodiments, the anti-NKG2D scFv and the IL2 are provided as a chimeric polypeptide. In some embodiments, the chimeric polypeptide further comprises a linker. In some embodiments, the anti-NKG2D scFv and the IL2 are provided as a fusion protein. In some embodiments, the fusion protein further comprises a linker. In some embodiments, the IL2 is a mutant R38A/F42K form of IL2. In certain embodiments, the subject is in need thereof. In certain embodiments, the subject is administered an effective amount of the combination therapy. In specific embodiments, the subject is a human. In certain embodiments, the subject is a subject having a cancer or tumor. In specific embodiments, the cancer or tumor is a lung cancer or tumor.

In an alternative aspect, the invention encompasses a method of use as an adjuvant in a vaccine composition. In one embodiment, provided herein is a method of vaccination in a subject, comprising administering to the subject a composition provided herein. In some embodiments, the method of vaccination in a subject comprises administering a chimeric peptide comprising a PD1 ligand and a cytokine. In another embodiment, the chimeric peptide further comprises a linker. In one embodiment, the PD1 ligand is PDL1. In another embodiment, the PD1 ligand is PDL2. In still another embodiment, the PD1 ligand is an antibody specific to PD1. In another embodiment, the cytokine is IL2. In some embodiments, the IL2 is a mutant R38A/F42K form of IL2. In one embodiment, provided herein is a method of vaccination in a subject, comprising administering to the subject a combination therapy provided herein. In some embodiments, the combination therapy includes a PD-1 inhibitor provided herein and a chimeric peptide that includes a cytokine peptide and an anti-NKG2D antibody. In certain embodiments, the cytokine peptide is a cytokine as described hereinabove. In some embodiments, the anti-NKG2D antibody is as described hereinabove. In one embodiment, the combination therapy comprises an OMCP-IL2 fusion protein and a PD-1 inhibitor. In another embodiment, the combination therapy comprises an OMCP-IL2 fusion protein and an anti-PD-1 antibody. In some embodiments, the fusion protein further comprises a linker. In one embodiment, the combination therapy comprises an OMCP-IL2 chimeric protein and a PD-1 inhibitor. In another embodiment, the combination therapy comprises an OMCP-IL2 chimeric protein and an anti-PD-1 antibody. In some embodiments, the chimeric protein further comprises a linker. In other embodiments, the combination therapy comprises an anti-NKG2D antibody, IL2 and a PD1 inhibitor. In some embodiments, the combination therapy comprises an anti-NKG2D antibody, IL2 and an anti-PD1 antibody. In some embodiment, the anti-PD-1 antibody is an antagonistic antibody. In certain embodiments, the anti-NKG2D antibody is KYK-1. In other embodiments, the anti-NKG2D antibody is KYK-2. In some embodiments, the anti-NKG2D antibody and the IL2 are provided as a chimeric polypeptide. In some embodiments, the chimeric polypeptide further comprises a linker. In some embodiments, the anti-NKG2D antibody and the IL2 are provided as a fusion protein. In some embodiments, the fusion protein further comprises a linker. In some embodiments, the combination therapy comprises an anti-NKG2D scFv, IL2 and a PD1 inhibitor. In some embodiments, the combination therapy comprises an anti-NKG2D scFv, IL2 and an anti-PD1 antibody. In some embodiment, the anti-PD-1 antibody is an antagonistic antibody. In certain embodiments, the anti-NKG2D scFv is a KYK-1 scFv. In other embodiments, the anti-NKG2D scFv is a KYK-2 scFv. In some embodiments, the anti-NKG2D scFv and the IL2 are provided as a chimeric polypeptide. In some embodiments, the chimeric polypeptide further comprises a linker. In some embodiments, the anti-NKG2D scFv and the IL2 are provided as a fusion protein. In some embodiments, the fusion protein further comprises a linker. In some embodiments, the IL2 is a mutant R38A/F42K form of IL2. In certain embodiments, the subject is in need thereof. In certain embodiments, the subject is administered an effective amount of the combination therapy. In specific embodiments, the subject is a human.

In other aspects, provided herein is a composition of the invention for use in expanding CD8+ memory cells. In one embodiment, provided herein is a method to expand CD8+ T cells in a subject, comprising administering to the subject a composition provided herein. In one embodiment, provided herein is a method to expand CD8+ T cells in a subject, the method further comprises administering a chimeric peptide comprising a PD1 ligand and a cytokine. In another embodiment, the chimeric peptide further comprises a linker. In one embodiment, the PD1 ligand is PDL1. In another embodiment, the PD1 ligand is PDL2. In still another embodiment, the PD1 ligand is an antibody specific to PD1. In another embodiment, the cytokine is IL2. In some embodiments, the IL2 is a mutant R38A/F42K form of IL2. In one embodiment, provided herein is a method to expand CD8+ T cells in a subject, comprising administering to the subject a combination therapy provided herein. In some embodiments, the combination therapy includes a PD-1 inhibitor provided herein and a chimeric peptide that includes a cytokine peptide and an anti-NKG2D antibody. In certain embodiments, the cytokine peptide is a cytokine as described hereinabove. In some embodiments, the anti-NKG2D antibody is as described hereinabove. In one embodiment, the combination therapy comprises an OMCP-IL2 fusion protein and a PD-1 inhibitor. In another embodiment, the combination therapy comprises an OMCP-IL2 fusion protein and an anti-PD-1 antibody. In some embodiments, the fusion protein further comprises a linker. In one embodiment, the combination therapy comprises an OMCP-IL2 chimeric protein and a PD-1 inhibitor. In another embodiment, the combination therapy comprises an OMCP-IL2 chimeric protein and an anti-PD-1 antibody. In some embodiments, the chimeric protein further comprises a linker. In other embodiments, the combination therapy comprises an anti-NKG2D antibody, IL2 and a PD1 inhibitor. In some embodiments, the combination therapy comprises an anti-NKG2D antibody, IL2 and an anti-PD1 antibody. In some embodiment, the anti-PD-1 antibody is an antagonistic antibody. In certain embodiments, the anti-NKG2D antibody is KYK-1. In other embodiments, the anti-NKG2D antibody is KYK-2. In some embodiments, the anti-NKG2D antibody and the IL2 are provided as a chimeric polypeptide. In some embodiments, the chimeric polypeptide further comprises a linker. In some embodiments, the anti-NKG2D antibody and the IL2 are provided as a fusion protein. In some embodiments, the fusion protein further comprises a linker. In some embodiments, the combination therapy comprises an anti-NKG2D scFv, IL2 and a PD1 inhibitor. In some embodiments, the combination therapy comprises an anti-NKG2D scFv, IL2 and an anti-PD1 antibody. In some embodiment, the anti-PD-1 antibody is an antagonistic antibody. In certain embodiments, the anti-NKG2D scFv is a KYK-1 scFv. In other embodiments, the anti-NKG2D scFv is a KYK-2 scFv. In some embodiments, the anti-NKG2D scFv and the IL2 are provided as a chimeric polypeptide. In some embodiments, the chimeric polypeptide further comprises a linker. In some embodiments, the anti-NKG2D scFv and the IL2 are provided as a fusion protein. In some embodiments, the fusion protein further comprises a linker. In some embodiments, the IL2 is a mutant R38A/F42K form of IL2. In certain embodiments, the subject is in need thereof. In certain embodiments, the subject is administered an effective amount of the combination therapy. In specific embodiments, the subject is a human. In certain embodiments, the subject is a subject having a cancer or tumor. In specific embodiments, the cancer or tumor is a lung cancer or tumor.

In other aspects, the disclosure provides a method to expand cytotoxic lympocytes ex vivo. The method comprises culturing lymphocytes in the presence of a composition provided herein. Lymphocytes may be derived from a publically available cell line, such as an ATCC™ cell line. Alternatively, lymphocytes may be isolated from a subject. The lymphocytes may be obtained from a single subject, or a plurality of subjects. A plurality refers to at least two (e.g., more than one) subjects. When lymphocytes obtained are from a plurality of subjects, their relationships may be autologous, syngeneic, allogeneic, or xenogeneic. Specifically, the lymphocytes may be cultured in the presence of a chimeric peptide described in Section I. In certain embodiments, the chimeric peptide comprises OMCP or a fragment thereof linked to IL2 or a mutant thereof. In other embodiments, the chimeric peptide comprises OMCP linked to mutant IL2. In another aspect, the disclosure provides a method to improve adoptive cellular immunotherapy in a subject. The method comprises administering to a subject a therapeutic composition comprising isolated cytotoxic lymphocytes that have been cultured in the presence of a composition provided herein. As used herein, “adoptive cellular immunotherapy”, also referred to as “ACI”, is a lymphocyte based immunotherapy whereby lympocytes are taken from a subject and stimulated and/or genetically manipulated. Following population expansion, the lymphocytes are then transferred back into the subject. Accordingly, the methods of the disclosure may be used to treat a disease or disorder in which it is desirable to increase the number of lymphocytes. For example, cancer and chronic viral infections. Regarding viral infections, ACI of virus-specific T cells may restore virus-specific immunity in a subject to prevent or treat viral diseases. Accordingly, virus-specific T cells may be used to reconstitute antiviral immunity after transplantation and/or to treat active viral infections. In an embodiment, a subject receiving T cells for treatment or prevention of a viral infection may be immunodeficient.

(a) Administration

In certain aspects, a pharmacologically effective amount of a composition of the invention may be administered to a subject. Administration is performed using standard effective techniques, including peripherally (i.e. not by administration into the central nervous system) or locally to the central nervous system. Peripheral administration includes but is not limited to intravenous, intraperitoneal, subcutaneous, pulmonary, transdermal, intramuscular, intranasal, buccal, sublingual, or suppository administration. Local administration, including directly into the central nervous system (CNS) includes but is not limited to via a lumbar, intraventricular or intraparenchymal catheter or using a surgically implanted controlled release formulation. Pheresis may be used to deliver a composition of the invention. In certain embodiments, a composition of the invention may be administered via an infusion (continuous or bolus).

Pharmaceutical compositions for effective administration are deliberately designed to be appropriate for the selected mode of administration, and pharmaceutically acceptable excipients such as compatible dispersing agents, buffers, surfactants, preservatives, solubilizing agents, isotonicity agents, stabilizing agents and the like are used as appropriate. Remington's Pharmaceutical Sciences, Mack Publishing Co., Easton Pa., 16Ed ISBN: 0-912734-04-3, latest edition, incorporated herein by reference in its entirety, provides a compendium of formulation techniques as are generally known to practitioners.

Effective peripheral systemic delivery by intravenous or intraperitoneal or subcutaneous injection is a preferred method of administration to a living patient. Suitable vehicles for such injections are straightforward. In addition, however, administration may also be effected through the mucosal membranes by means of nasal aerosols or suppositories. Suitable formulations for such modes of administration are well known and typically include surfactants that facilitate cross-membrane transfer. Such surfactants are often derived from steroids or are cationic lipids, such as N-[1-(2,3-dioleoyl)propyl]-N,N,N-trimethyl ammonium chloride (DOTMA) or various compounds such as cholesterol hemisuccinate, phosphatidyl glycerols and the like.

For therapeutic applications, a therapeutically effective amount of a composition of the invention is administered to a subject. A “therapeutically effective amount” is an amount of the therapeutic composition sufficient to produce a measurable response (e.g., an immunostimulatory, an anti-angiogenic response, a cytotoxic response, tumor regression, immunoinhibitory, immunosuppression, infection reduction). Actual dosage levels of active ingredients in a therapeutic composition of the invention can be varied so as to administer an amount of the active compound(s) that is effective to achieve the desired therapeutic response for a particular subject. The selected dosage level will depend upon a variety of factors including the activity of the therapeutic composition, formulation, the route of administration, combination with other drugs or treatments, tumor size and longevity, the autoimmune disease, infection, and the physical condition and prior medical history of the subject being treated. In some embodiments, a minimal dose is administered, and dose is escalated in the absence of dose-limiting toxicity. Determination and adjustment of a therapeutically effective dose, as well as evaluation of when and how to make such adjustments, are known to those of ordinary skill in the art of medicine. In an aspect, a typical dose contains from about 10 IU/kg to about 1,000,000 IU/kg of a cytokine described herein. In an embodiment, a typical dose contains from about 10 IU/kg to about 100 IU/kg. In another embodiment, a typical dose contains about 100 IU/kg to about 1,000 IU/kg. In still another embodiment, a typical dose contains about 1,000 IU/kg to about 10,000 IU/kg. In yet still another embodiment, a typical dose contains about 10,000 IU/kg to about 100,000 IU/kg. In a different embodiment, a typical dose contains about 100,000 IU/kg to about 1,000,000 IU/kg. In certain embodiments, a typical dose contains about 500,000 IU/kg to about 1,000,000 IU/kg. In other embodiments, a typical dose contains about 100,000 IU/kg to about 500,000 IU/kg. Alternatively, a typical dose contains about 50,000 IU/kg to about 100,000 IU/kg. In another embodiment, a typical dose contains about 10,000 IU/kg to about 50,000 IU/kg. In still another embodiment, a typical dose contains about 5,000 IU/kg to about 10,000 IU/kg. In a specific embodiment, a typical dose contains about 5,000 IU/kg to about 200,000 IU/kg. In another specific embodiment, a typical dose contains about 5,000 IU/kg to about 500,000 IU/kg. In still another specific embodiment, a typical dose contains about 50,000 IU/kg to about 500,000 IU/kg. In still yet another specific embodiment, a typical dose contains about 250,000 IU/kg to about 750,000 IU/kg.

The frequency of dosing may be once, twice, three times or more daily or once, twice, three times or more per week or per month, as needed as to effectively treat the symptoms or disease. In certain embodiments, the frequency of dosing may be once, twice or three times daily. For example, a dose may be administered every 24 hours, every 12 hours, or every 8 hours. In a specific embodiment, the frequency of dosing may be twice daily.

Duration of treatment could range from a single dose administered on a one-time basis to a life-long course of therapeutic treatments. The duration of treatment can and will vary depending on the subject and the cancer or autoimmune disease or infection to be treated. For example, the duration of treatment may be for 1 day, 2 days, 3 days, 4 days, 5 days, 6 days, or 7 days. Or, the duration of treatment may be for 1 week, 2 weeks, 3 weeks, 4 weeks, 5 weeks or 6 weeks. Alternatively, the duration of treatment may be for 1 month, 2 months, 3 months, 4 months, 5 months, 6 months, 7 months, 8 months, 9 months, 10 months, 11 months, or 12 months. In still another embodiment, the duration of treatment may be for 1 year, 2 years, 3 years, 4 years, 5 years, or greater than 5 years. It is also contemplated that administration may be frequent for a period of time and then administration may be spaced out for a period of time. For example, duration of treatment may be 5 days, then no treatment for 9 days, then treatment for 5 days.

The timing of administration of the treatment relative to the disease itself and duration of treatment will be determined by the circumstances surrounding the case. Treatment could begin immediately, such as at the time of diagnosis, or treatment could begin following surgery. Treatment could begin in a hospital or clinic itself, or at a later time after discharge from the hospital or after being seen in an outpatient clinic.

Furthermore, treatment with a composition as described above can begin in an administration regimen together (e.g., sequentially or simultaneously) with administration of a PD-1 inhibitor or PD-L1 inhibitor described herein. In some embodiments, the PD-L1 inhibitor is present in an amount as a measure with regards to the weight of the patient in need thereof. For example, in some embodiments, the PD-L1 inhibitor is present in an amount of about: 0.1 mg/kg to about 50 mg/kg, 0.1 mg/kg to about 40 mg/kg, 0.1 mg/kg to about 30 mg/kg, 0.1 mg/kg to about 25 mg/kg, 0.1 mg/kg to about 20 mg/kg, 0.1 mg/kg to about 15 mg/kg, 0.1 mg/kg to about 10 mg/kg, 0.1 mg/kg to about 7.5 mg/kg, 0.1 mg/kg to about 5 mg/kg, 0.1 mg/kg to about 2.5 mg/kg, or about 0.1 mg/kg to about 1 mg/kg. In some embodiments, the PD-L1 inhibitor is present in an amount of about: 0.5 mg/kg to about 50 mg/kg, 0.5 mg/kg to about 40 mg/kg, 0.5 mg/kg to about 30 mg/kg, 0.5 mg/kg to about 25 mg/kg, 0.5 mg/kg to about 20 mg/kg, 0.5 mg/kg to about 15 mg/kg, 0.5 mg/kg to about 10 mg/kg, 0.5 mg/kg to about 7.5 mg/kg, 0.5 mg/kg to about 5 mg/kg, 0.5 mg/kg to about 2.5 mg/kg, or about 0.5 mg/kg to about 1 mg/kg. In some embodiments, the PD-L1 inhibitor is present in an amount of about 0.5 mg/kg to about 5 mg/kg or about 0.1 mg/kg to about 10 mg/kg. In some embodiments, the PD-L1 inhibitor is present in an amount of about 0.1 mg/kg to about 20 mg/kg or about 0.1 mg/kg to about 30 mg/kg.

In still other embodiments, In some embodiments, the PD-L1 inhibitor is present at an amount of about: 0.1 mg/kg, 0.5 mg/kg, 1 mg/kg, 2 mg/kg, 3 mg/kg, 4 mg/kg, 5 mg/kg, 10 mg/kg, 15 mg/kg, 20 mg/kg, 25 mg/kg, 30 mg/kg, 35 mg/kg, 40 mg/kg, or 50 mg/kg. The PD-L1 antibody can be present at an amount of about: 1 mg/kg, 2 mg/kg, 3 mg/kg, 5 mg/kg, 10 mg/kg, 15 mg/kg, 20 mg/kg, 25 mg/kg, or 30 mg/kg. In some embodiments, the PD-L1 inhibitor is present at an amount of about: 3 mg/kg, 10 mg/kg, 20 mg/kg, or 30 mg/kg.

In some embodiments, the PD-L1 inhibitor is present in the combination therapy at an amount of about: 1 mg, 5 mg, 10 mg, 15 mg, 20 mg, 25 mg, 30 mg, 40 mg, 50 mg, 60 mg, 70 mg, 75 mg, 80 mg, 90 mg, 100 mg, 150 mg, or 200 mg. In some embodiments, the PD-L1 inhibitor is present in the combination therapy at an amount of about: 250 mg, 300 mg, 400 mg, 500 mg, 600 mg, 700 mg, 800 mg, 900 mg, 1000 mg, 1100 mg, 1200 mg, 1300 mg, 1400 mg, 1500 mg, 1600 mg, 1700 mg, 1800 mg, 1900 mg, or 2000 mg. In some embodiments, the PD-L1 inhibitor is present in the combination therapy at an amount of about 1000 mg to about 2000 mg. In some embodiments, the PD-L1 inhibitor is present in the combination therapy at an amount of about: 1 mg to about 10 mg, 10 mg to about 20 mg, 25 mg to about 50 mg, 30 mg to about 60 mg, 40 mg to about 50 mg, 50 mg to about 100 mg, 75 mg to about 150 mg, 100 mg to about 200 mg, 200 mg to about 500 mg, 500 mg to about 1000 mg, 1000 mg to about 1200 mg, 1000 mg to about 1500 mg, 1200 mg to about 1500 mg, or 1500 to about 2000 mg.

In some embodiments, the PD-L1 inhibitor is present in the combination therapy in an amount of about 0.1 mg/mL, 0.5 mg/mL, 1 mg/mL, 2 mg/mL, 3 mg/mL, 4 mg/mL, 5 mg/mL, 6 mg/mL, 7 mg/mL, 8 mg/mL, 9 mg/mL, 10 mg/mL, 15 mg/mL, 20 mg/mL, 25 mg/mL, 30 mg/mL, 40 mg/mL, 50 mg/mL, 60 mg/mL, 70 mg/mL, 80 mg/mL, 90 mg/mL, 100 mg/mL, 150 mg/mL, 200 mg/mL, 250 mg/mL, 300 mg/mL, 400 mg/mL, or 500 mg/mL. In one embodiment, the PD-L1 inhibitor is present in the combination therapy in an amount of about: 1 mg/mL to about 10 mg/mL, 5 mg/mL to about 10 mg/mL, 5 mg/mL to about 15 mg/mL, 10 mg/mL to about 25 mg/mL; 20 mg/mL to about 30 mg/mL; 25 mg/mL to about 50 mg/mL, or 50 mg/mL to about 100 mg/mL.

In certain instances the therapeutically effective amount of a PD-L1 inhibitor is determined as an amount provided in a package insert provided with the PD-L1 inhibitor. The term package insert refers to instructions customarily included in commercial packages of medicaments approved by the FDA or a similar regulatory agency of a country other than the USA, which contains information about, for example, the usage, dosage, administration, contraindications, and/or warnings concerning the use of such medicaments.

In some embodiments, the PD-1 inhibitor is present in an amount as a measure with regards to the weight of the patient in need thereof. For example, in some embodiments, the PD-1 inhibitor is present in an amount of about: 0.1 mg/kg to about 30 mg/kg, 0.1 mg/kg to about 25 mg/kg, 0.1 mg/kg to about 20 mg/kg, 0.1 mg/kg to about 15 mg/kg, 0.1 mg/kg to about 10 mg/kg, 0.1 mg/kg to about 7.5 mg/kg, 0.1 mg/kg to about 5 mg/kg, 0.1 mg/kg to about 2.5 mg/kg, or about 0.1 mg/kg to about 1 mg/kg. In some embodiments, the PD-1 inhibitor is present in an amount of about: 0.5 mg/kg to about 30 mg/kg, 0.5 mg/kg to about 25 mg/kg, 0.5 mg/kg to about 20 mg/kg, 0.5 mg/kg to about 15 mg/kg, 0.5 mg/kg to about 10 mg/kg, 0.5 mg/kg to about 7.5 mg/kg, 0.5 mg/kg to about 5 mg/kg, 0.5 mg/kg to about 2.5 mg/kg, or about 0.5 mg/kg to about 1 mg/kg. In some embodiments, the PD-1 inhibitor is present in an amount of about 0.5 mg/kg to about 5 mg/kg or about 0.1 mg/kg to about 10 mg/kg. In some embodiments, the PD-1 inhibitor is present in an amount of about 0.5 mg/kg to about 15 mg/kg or about 0.1 mg/kg to about 20 mg/kg.

In some embodiments, the PD-1 inhibitor is present at an amount of about: 0.1 mg/kg, 0.5 mg/kg, 1 mg/kg, 2 mg/kg, 3 mg/kg, 4 mg/kg, 5 mg/kg, 10 mg/kg, 15 mg/kg, 20 mg/kg or 30 mg/kg. In some embodiments, the PD-1 inhibitor is present at an amount of about: 1 mg/kg, 2 mg/kg, 3 mg/kg, or 5 mg/kg.

In some embodiments, the PD-1 inhibitor is present in the combination therapy at an amount of about: 1 mg, 5 mg, 10 mg, 15 mg, 20 mg, 25 mg, 30 mg, 40 mg, 50 mg, 60 mg, 70 mg, 75 mg, 80 mg, 90 mg, 100 mg, 150 mg, 200 mg, 250 mg, 300 mg, 400 mg, 500 mg, 600 mg, 700 mg, 800 mg, 900 mg, 1000 mg, 1100 mg, 1200 mg, 1300 mg, 1400 mg, 1500 mg, 1600 mg, 1700 mg, 1800 mg, 1900 mg, or 2000 mg. In some embodiments, the PD-1 inhibitor is present in the combination therapy at an amount of about: 1 mg to about 10 mg, 10 mg to about 20 mg, 25 mg to about 50 mg, 30 mg to about 60 mg, 40 mg to about 50 mg, 50 mg to about 100 mg, 75 mg to about 150 mg, 100 mg to about 200 mg, 200 mg to about 500 mg, 500 mg to about 1000 mg, 1000 mg to about 1200 mg, 1000 mg to about 1500 mg, 1200 mg to about 1500 mg, or 1500 mg to about 2000 mg.

In some embodiments, the PD-1 inhibitor is present in the combination therapy in an amount of about: 0.1 mg/mL, 0.5 mg/mL, 1 mg/mL, 2 mg/mL, 3 mg/mL, 4 mg/mL, 5 mg/mL, 6 mg/mL, 7 mg/mL, 8 mg/mL, 9 mg/mL, 10 mg/mL, 15 mg/mL, 20 mg/mL, 25 mg/mL, 30 mg/mL, 40 mg/mL, 50 mg/mL, 60 mg/mL, 70 mg/mL, 80 mg/mL, 90 mg/mL, 100 mg/mL, 150 mg/mL, 200 mg/mL, 250 mg/mL, 300 mg/mL, 400 mg/mL, or 500 mg/mL. In one embodiment, the PD-1 inhibitor is present in the combination therapy in an amount of about: 1 mg/mL to about 10 mg/mL, 5 mg/mL to about 10 mg/mL, 5 mg/mL to about 15 mg/mL, 10 mg/mL to about 25 mg/mL; 20 mg/mL to about 30 mg/mL; 25 mg/mL to about 50 mg/mL, or 50 mg/mL to about 100 mg/mL.

In certain instances the therapeutically effective amount of a PD-1 inhibitor is determined as an amount provided in a package insert provided with the PD-1 inhibitor.

A synergistic effect of a combination therapy described herein can permit the use of lower dosages of one or more of the components of the combination (e.g., a composition described herein and a PD-1 or PD-L1 inhibitor). A synergistic effect can permit less frequent administration of at least one of the administered therapies (e.g., a composition described herein and a PD-1 or PD-L1 inhibitor) to a subject with a disease, disorder, or condition described herein. Such lower dosages and reduced frequency of administration can reduce the toxicity associated with the administration of at least one of the therapies (e.g., a composition described herein and a PD-1 or PD-L1 inhibitor) to a subject without reducing the efficacy of the treatment. A synergistic effect as described herein can avoid or reduce adverse or unwanted side effects associated with the use of either of the therapies described herein.

Although the foregoing methods appear the most convenient and most appropriate and effective for administration of a composition or a combination therapy of the invention, by suitable adaptation, other effective techniques for administration, such as intraventricular administration, transdermal administration and oral administration may be employed provided proper formulation is utilized herein.

In addition, it may be desirable to employ controlled release formulations using biodegradable films and matrices, or osmotic mini-pumps, or delivery systems based on dextran beads, alginate, or collagen.

(b) Tumor

A composition of the invention may be used in a method to treat or recognize a tumor derived from a neoplasm or a cancer. The neoplasm may be malignant or benign, the cancer may be primary or metastatic; the neoplasm or cancer may be early stage or late stage. Non-limiting examples of neoplasms or cancers that may be treated include acute lymphoblastic leukemia, acute myeloid leukemia, adrenocortical carcinoma, AIDS-related cancers, AIDS-related lymphoma, anal cancer, appendix cancer, astrocytomas (childhood cerebellar or cerebral), basal cell carcinoma, bile duct cancer, bladder cancer, bone cancer, brainstem glioma, brain tumors (cerebellar astrocytoma, cerebral astrocytoma/malignant glioma, ependymoma, medulloblastoma, supratentorial primitive neuroectodermal tumors, visual pathway and hypothalamic gliomas), breast cancer, bronchial adenomas/carcinoids, Burkitt lymphoma, carcinoid tumors (childhood, gastrointestinal), carcinoma of unknown primary, central nervous system lymphoma (primary), cerebellar astrocytoma, cerebral astrocytoma/malignant glioma, cervical cancer, childhood cancers, chronic lymphocytic leukemia, chronic myelogenous leukemia, chronic myeloproliferative disorders, colon cancer, cutaneous T-cell lymphoma, desmoplastic small round cell tumor, endometrial cancer, ependymoma, esophageal cancer, Ewing's sarcoma in the Ewing family of tumors, extracranial germ cell tumor (childhood), extragonadal germ cell tumor, extrahepatic bile duct cancer, eye cancers (intraocular melanoma, retinoblastoma), gallbladder cancer, gastric (stomach) cancer, gastrointestinal carcinoid tumor, gastrointestinal stromal tumor, germ cell tumors (childhood extracranial, extragonadal, ovarian), gestational trophoblastic tumor, gliomas (adult, childhood brain stem, childhood cerebral astrocytoma, childhood visual pathway and hypothalamic), gastric carcinoid, hairy cell leukemia, head and neck cancer, hepatocellular (liver) cancer, Hodgkin lymphoma, hypopharyngeal cancer, hypothalamic and visual pathway glioma (childhood), intraocular melanoma, islet cell carcinoma, Kaposi sarcoma, kidney cancer (renal cell cancer), laryngeal cancer, leukemias (acute lymphoblastic, acute myeloid, chronic lymphocytic, chronic myelogenous, hairy cell), lip and oral cavity cancer, liver cancer (primary), lung cancers (non-small cell, small cell), lymphomas (AIDS-related, Burkitt, cutaneous T-cell, Hodgkin, non-Hodgkin, primary central nervous system), macroglobulinemia (Waldenström), malignant fibrous histiocytoma of bone/osteosarcoma, medulloblastoma (childhood), melanoma, intraocular melanoma, Merkel cell carcinoma, mesotheliomas (adult malignant, childhood), metastatic squamous neck cancer with occult primary, mouth cancer, multiple endocrine neoplasia syndrome (childhood), multiple myeloma/plasma cell neoplasm, mycosis fungoides, myelodysplastic syndromes, myelodysplastic/myeloproliferative diseases, myelogenous leukemia (chronic), myeloid leukemias (adult acute, childhood acute), multiple myeloma, myeloproliferative disorders (chronic), nasal cavity and paranasal sinus cancer, nasopharyngeal carcinoma, neuroblastoma, non-Hodgkin lymphoma, non-small cell lung cancer, oral cancer, oropharyngeal cancer, osteosarcoma/malignant fibrous histiocytoma of bone, ovarian cancer, ovarian epithelial cancer (surface epithelial-stromal tumor), ovarian germ cell tumor, ovarian low malignant potential tumor, pancreatic cancer, pancreatic cancer (islet cell), paranasal sinus and nasal cavity cancer, parathyroid cancer, penile cancer, pharyngeal cancer, pheochromocytoma, pineal astrocytoma, pineal germinoma, pineoblastoma and supratentorial primitive neuroectodermal tumors (childhood), pituitary adenoma, plasma cell neoplasia, pleuropulmonary blastoma, primary central nervous system lymphoma, prostate cancer, rectal cancer, renal cell carcinoma (kidney cancer), renal pelvis and ureter transitional cell cancer, retinoblastoma, rhabdomyosarcoma (childhood), salivary gland cancer, sarcoma (Ewing family of tumors, Kaposi, soft tissue, uterine), Sezary syndrome, skin cancers (nonmelanoma, melanoma), skin carcinoma (Merkel cell), small cell lung cancer, small intestine cancer, soft tissue sarcoma, squamous cell carcinoma, squamous neck cancer with occult primary (metastatic), stomach cancer, supratentorial primitive neuroectodermal tumor (childhood), T-Cell lymphoma (cutaneous), testicular cancer, throat cancer, thymoma (childhood), thymoma and thymic carcinoma, thyroid cancer, thyroid cancer (childhood), transitional cell cancer of the renal pelvis and ureter, trophoblastic tumor (gestational), unknown primary site (adult, childhood), ureter and renal pelvis transitional cell cancer, urethral cancer, uterine cancer (endometrial), uterine sarcoma, vaginal cancer, visual pathway and hypothalamic glioma (childhood), vulvar cancer, Waldenström macroglobulinemia, and Wilms tumor (childhood). In certain embodiments, the neoplasm or cancer may be selected from the group consisting of melanoma, renal cell carcinoma, lung cancer and blood cancer. In one embodiment, the tumor is melanoma. In another embodiment, the tumor is renal cell carcinoma. In one embodiment, the tumor is lung cancer (e.g., NSCLC). In another embodiment, the tumor is a blood cancer described herein. As used herein, a “blood cancer” is a cancer that affects the blood, bone marrow and lymphatic system. There are three main groups of blood cancer: leukemia, lymphoma and myeloma. The four broad classification of leukemia are: acute lymphocytic leukemia (ALL), acute myelogenous leukemia (AML), chronic lymphocytic leukemia (CLL) and chronic myelogenous leukemia (CML). Lymphomas are divided into two categories: Hodgkin lymphoma and non-Hodgkin lymphoma. Most non-Hodgkin lymphomas are B-cell lymphomas, and either grow quickly (high-grade) or slowly (low-grade). There are 14 types of B-cell non-Hodgkin lymphomas. The rest are T-cell lymphomas, named after a different cancerous white blood cell, or lymphocyte. Because myeloma frequently occurs at many sites in the bone marrow, it is often referred to as multiple myeloma. In some embodiments, the method comprises administration of a combination therapy as provided herein. In some embodiments, the combination therapy comprises a PD-1 inhibitor. In other embodiments, the PD-1 inhibitor is an anti-PD-1 antibody. In some embodiments, the combination therapy comprises a PD-L1 inhibitor. In other embodiments, the PD-L1 inhibitor is an anti-PD-L1 antibody.

(c) Subject

A suitable subject includes a human, a livestock animal, a companion animal, a lab animal, or a zoological animal. In one embodiment, the subject may be a rodent, e.g. a mouse, a rat, a guinea pig, etc. In another embodiment, the subject may be a livestock animal. Non-limiting examples of suitable livestock animals may include pigs, cows, horses, goats, sheep, llamas and alpacas. In yet another embodiment, the subject may be a companion animal. Non-limiting examples of companion animals may include pets such as dogs, cats, rabbits, and birds. In yet another embodiment, the subject may be a zoological animal. As used herein, a “zoological animal” refers to an animal that may be found in a zoo. Such animals may include non-human primates, large cats, wolves, and bears. In a specific embodiment, the animal is a laboratory animal. Non-limiting examples of a laboratory animal may include rodents, canines, felines, and non-human primates. In certain embodiments, the animal is a rodent. Non-limiting examples of rodents may include mice, rats, guinea pigs, etc. In preferred embodiments, the subject is a human.

TABLE A
Sequences

SEQ
ID NO	Name	Sequence	Source

1	R38A,	CACAAACTCGCATTCAACTTCAATCTAGAAATAAATGGCAG	Synthesized
	F42K,	TGATACACATTCTACAGTAGATGTATATCTTGATGATTCT
	C125S IL2-	CAAATTATAACGTTTGATGGAAAAGATATCCGTCCAA
	OMCP	CCATCCCGTTCATGATAGGTGATGAAATTTTCTTACCGTTT
	construct	TATAAAAATGTGTTTAGTGAGTTTTTCTCTCTGTTTAGAAGA
		GTTCCTACAAGTACTCCATATGAAGACTTGACATATTTTTAT
		GAATGCGACTATACAGACAATAAATCTACATTTGATCAGTT
		TTATCTTTATAATGGCGAAGAATATACTGTCAAAACACAGG
		AGGCCACTAATAAAAATATGTGGCTAACTACTTCCGAGTTT
		AGACTAAAAAAATGGTTCGATGGCGAAGATTGTATAATGCA
		TCTTAGATCGTTAGTTAGAAAAATGGAGGACAGTAAACGAA
		ACACTGGTGGTACCGGAAGTAGCGGTAGTAGTGATTACAA
		GGACGATGACGACAAGCACCACCATCATCATCATCACCAC
		GGTAGCAGCGGCAGCAGTGCCCCCACCTCTAGCAGCACA
		AAGAAGACCCAGCTGCAACTGGAACACCTCCTGCTGGACC
		TGCAGATGATCCTGAACGGCATCAACAACTACAAGAACCC
		CAAGCTGACCGCCATGCTGACCAAAAAGTTTTACATGCCC
		AAGAAGGCCACCGAGCTTAAACACCTGCAATGCCTTGAGG
		AGGAGCTGAAGCCCTGGAGGAGGTACTGAACCTGGCCCA
		GAGCAAGAACTTTCATCTGAGGCCCAGGGACCTGATTAGC
		AACATCAACGTGATCGTGTTGGAGTTGAAGGGCAGCGAGA
		CCACGTTCATGTGCGAGTACGCCGACGAGACGGCCACCA
		TAGTGGAGTTTCTTAACAGGTGGATCACCTTCTCACAGTCT
		ATCATCAGCACCCTGACC
2	R38A,	HKLAFNFNLEINGSDTHSTVDVYLDDSQIITFDGKDIRPTIPFMI	Synthesized
	F42K,	GDEIFLPFYKNVFSEFFSLFRRVPTSTPYEDLTYFYECDYTDN
	C125S IL2-	KSTFDQFYLYNGEEYTVKTQEATNKNMWLTTSEFRLKKWFD
	OMCP	GEDCIMHLRSLVRKMEDSKRNTGGTGSSGSSDYKDDDDKH
	construct	HHHHHHHGSSGSSAPTSSSTKKTQLQLEHLLLDLQMILNGIN
		NYKNPKLTAMLTKKFYMPKKATELKHLQCLEEELKPLEEVLN
		LAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIV
		EFLNRWITFSQSIISTLT
3	Melanoma	SVYDFFVWL	Homo sapiens
	tumor
	associate
	antigen
	tyrosinase-
	related
	protein 2
	peptide
4	Highly	SIINFEKL	Homo sapiens
	immunogenic
	peptide
5	WT IL2	APTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFK	Homo sapiens
	(C125S)	FYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLI
		SNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFCQSIIST
		LT
6	R38A,	APTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTAMLTKK	Synthesized
	F42K,	FYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLI
	C125S IL2	SNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFSQSIIST
		LT
7	OMCP	HKLAFNFNLEINGSDTHSTVDVYLDDSQIITFDGKDIRPTIPFMI	Synthesized
		GDEIFLPFYKNVFSEFFSLFRRVPTSTPYEDLTYFYECDYTDN
		KSTFDQFYLYNGEEYTVKTQEATNKNMWLTTSEFRLKKWFD
		GEDCIMHLRSLVRKMEDSKRNTG
8	Linker	GSSGSSDYKDDDDKHHHHHHHHGSSGSS	Synthesized
9	FLAG tag	DYKDDDK	Synthesized
10	HA tag	YPYDVPDYA	Synthesized
11	Myc tag	EQKLISEEDL	Synthesized
12	V5 tag	GKPIPNPLLGLDST	Synthesized
13	OMCPbr	GHKLAFNFNLEINGSDTHSTVDVYLDDSQIITFDGKDIRPTIPF	Cowpox virus
		MIGDEIFLPFYKNVFSEFFSLFRRVPTSTPYEDLTYFYECDYT
		DNKSTFDQFYLYNGEEYTVKTQEATNKNMWLTTSEFRLKKW
		FDGEDCIMHLRSLVRKMEDSKR
14	OMCPmpx	HKLVHYFNLKINGSDITNTADILLDNYPIMTFDGKDIYPSIAFMV	Monkeypox
		GNKLFLDLYKNIFVEFFRLFRVSVSSQYEELEYYYSCDYTNN	virus
		RPTIKQHYFYNGEEYTEIDRSKKATNKNSWLITSGFRLQKWF
		DSEDCIIYLRSLVRRMEDSNK
15	MICA	MEPHSLRYNLTVLSWDGSVQSGFLTEVHLDGQPFLRCRDR	Homo sapiens
		QKCRAKPQGQWAEDVLGNKTWDRETRDLTGNGKDLRMTLA
		HIKDQKEGLHSLQEIRVCEIHEDNSTRSSQHFYYDGELFLSQ
		NLETKEWTMPQSSRAQTLAMNVRNFLKEDAMKTKTHYHAM
		HADCLQELRRYLKSGVVLR
16	MICB	MEPHSLRYNLMVLSQDGSVQSGFLAEGHLDGQPFLRYDRQ	Homo sapiens
		KRRAKPQGQWAEDVLGAETWDTETEDLTENGQDLRRTLTHI
		KDQKGGLHSLQEIRVCEIHEDSSTRGSRHFYYNGELFLSQNL
		ETQESTVPQSSRAQTLAMNVTNFWKEDAMKTKTHYRAMQA
		DCLQKLQRYLKSGVAIR
17	ULBP3	DAHSLWYNFTIIHLPRHGQQWCEVQSQVDQKNFLSYDCGSD	Homo sapiens
		KVLSMGHLEEQLYATDAWGKQLEMLREVGQRLRLELADTEL
		EDFTPSGPLTLQVRMSCECEADGYIRGSWQFSFDGRKFLLF
		DSNNRKWTVVHAGARRMKEKWEKDSGLTTFFKMVSMRDCK
		SWLRDFLMHRKKRLE
18	RAE-1B	DAHSLRCNLTIKDPTPADPLWYEAKCFVGEILILHLSNINKTMT	Homo sapiens
		SGDPGETANATEVKKCLTQPLKNLCQKLRNKVSNTKVDTHK
		TNGYPHLQVTMIYPQSQGRTPSATWEFNISDSYFFTFYTENM
		SWRSANDESGVIMNKWKDDGEFVKQLKFLIHECSQKMDEFL
		KQSKEK
19	NKG2D	LTIIEMQKGDCALYAS	Homo sapiens
	portion
20	NKG2D	LTIIEMQKGECALYAS	Green monkey
	portion
21	NKG2D	LTIIEMQKGDCAVYAS	Marmoset
	portion
22	NKG2D	LTLVEIPKGSCAVYGS	Mouse
	portion
23	NKG2D	LTLVKTPSGTCAVYGS	Rat
	portion
24	NKG2D	LTLMDTQNGKCALYGS	Guinea pig
	portion
25	NKG2D	LTLVEMQNGTCIVYGS	Ground
	portion		squirrel
26	NKG2D	LTVVEMQSGSCAVYGS	Deer mouse
	portion
27	NKG2D	LSMVEMQNGTCAVYAS	Naked mole
	portion		rat
28	NKG2D	LTLVEMQRGSCAVYGS	Prairie vole
	portion
29	NKG2D	VSIVEMQGGNCAVYGS	European
	portion		shrew
30	NKG2D	VTVYEMQNGSCAVYGS	Star-nosed
	portion		mole
31	NKG2D	LTLVEMQNGSCAVYGS	Chinese
	portion		hamster
32	NKG2D	LTMVDMQNGTCAVYGS	Cat
	portion
33	OMCP	ASSFK	Cowpox virus
	portion
34	DAP10	YINM	Synthesized
	signaling
	motif
35	KYK-1	QPVLTQPSSVSVAPGETARIPCGGDDIETKSVHWYQQKPGQ	Synthesized
	antibody	APVLVIYDDDDRPSGIPERFFGSNSGNTATLSISRVEAGDEAD
	(light chain)	YYC QVWDDNNDEWV FGGGTQLTVL
36	KYK-1	EVQLVESGGGVVQPGGSLRLSCAASGFTFSSYGMHWVRQA	Synthesized
	antibody	PGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQ
	(heavy	MNSLRAEDTAVYYCAK DRFGYYLDY WGQGTLVTVSS
	chain)
37	KYK-2	QSALTQPASVSGSPGQSITISCSGSSSNIGNNAVNWYQQLP	Synthesized
	antibody	GKAPKLLIYYDDLLPSGVSDRFSGSKSGTSAFLAISGLQSEDE
	(light chain)	ADYYC AAWDDSLNGPV FGGGTKLTVL
38	KYK-2	QVQLVESGGGLVKPGGSLRLSCAASGFTFSSYGMHWRQA	Synthesized
	antibody	PGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQ
	(heavy	MNSLRAEDTAVYYCAK DRGLGDGTYFDYWGQGTTVTVSS
	chain)
39	KYK-1 scFv	QPVLTQPSSVSVAPGETARIPCGGDDIETKSVHWYQQKPGQ	Synthesized
	1	APVLVIYDDDDRPSGIPERFFGSNSGNTATLSISRVEAGDEAD
		YYCQVWDDNNDEWVFGGGTQLTVLGGGGSGGGGSGGGG
		SGGGGSEVQLVESGGGVVQPGGSLRLSCAASGFTFSSYGM
		HWVRQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNS
		KNTLYLQMNSLRAEDTAVYYCAKDRFGYYLDYWGQGTLVTV
		SS
40	KYK-1 scFv	EVQLVESGGGVVQPGGSLRLSCAASGFTFSSYGMHWVRQA	Synthesized
	2	PGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQ
		MNSLRAEDTAVYYCAKDRFGYYLDYWGQGTLVTVSSGGGG
		SGGGGSGGGGSGGGGSQPVLTQPSSVSVAPGETARIPCGG
		DDIETKSVHWYQQKPGQAPVLVIYDDDDRPSGIPERFFGSNS
		GNTATLSISRVEAGDEADYYCQVWDDNNDEWVFGGGTQLT
		VL
41	KYK-2 scFv	QSALTQPASVSGSPGQSITISCSGSSSNIGNNAVNWYQQLP	Synthesized
	1	GKAPKLLIYYDDLLPSGVSDRFSGSKSGTSAFLAISGLQSEDE
		ADYYCAAWDDSLNGPVFGGGTKLTVLGGGGSGGGGSGGG
		GSGGGGSQVQLVESGGGLVKPGGSLRLSCAASGFTFSSYG
		MHWVRQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDN
		SKNTLYLQMNSLRAEDTAVYYCAKDRGLGDGTYFDYWGQG
		TTVTVSS
42	KYK-2 scFv	QVQLVESGGGLVKPGGSLRLSCAASGFTFSSYGMHWRQA	Synthesized
	2	PGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLYLQ
		MNSLRAEDTAVYYCAKDRGLGDGTYFDYWGQGTTVTV
43	R38A,	QPVLTQPSSVSVAPGETARIPCGGDDIETKSVHWYQQKPGQ	Synthesized
	F42K,	APVLVIYDDDDRPSGIPERFFGSNSGNTATLSISRVEAGDEAD
	C125S IL2-	YYCQVWDDNNDEWVFGGGTQLTVLGGGGSGGGGSGGGG
	KYK-1 (light-	SGGGGSEVQLVESGGGVVQPGGSLRLSCAASGFTFSSYGM
	heavy)	HWVRQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNS
	construct	KNTLYLQMNSLRAEDTAVYYCAKDRFGYYLDYWGQGTLVTV
		SSGGSSGSSGSSHHHHHHHHGGSSGSSGSSAPTSSSTKKT
		QLQLEHLLLDLQMILNGINNYKNPKLTAMLTKKFYMPKKATEL
		KHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELK
		GSETTFMCEYADETATIVEFLNRWITFSQSIISTLT
44	R38A,	EVQLVESGGGVVQPGGSLRLSCAASGFTFSSYGMHWVRQ	Synthesized
	F42K,	APGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLY
	C125S IL2-	LQMNSLRAEDTAVYYCAKDRFGYYLDYWGQGTLVTVSSGG
	KYK-1	GGSGGGGSGGGGSGGGGSQPVLTQPSSVSVAPGETARIP
	(heavy-light)	CGGDDIETKSVHWYQQKPGQAPVLVIYDDDDRPSGIPERFF
	construct	GSNSGNTATLSISRVEAGDEADYYCQVWDDNNDEWVFGGG
		TQLTVLGGSSGSSGSSHHHHHHHHGGSSGSSGSSAPTSSS
		TKKTQLQLEHLLLDLQMILNGINNYKNPKLTAMLTKKFYMPKK
		ATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIV
		LELKGSETTFMCEYADETATIVEFLNRWITFSQSIISTLT
45	R38A,	QSALTQPASVSGSPGQSITISCSGSSSNIGNNAVNWYQQLP	Synthesized
	F42K,	GKAPKLLIYYDDLLPSGVSDRFSGSKSGTSAFLAISGLQSED
	C125S IL2-	EADYYCAAWDDSLNGPVFGGGTKLTVLGGGGSGGGGSGG
	KYK-2 (light-	GGSGGGGSQVQLVESGGGLVKPGGSLRLSCAASGFTFSSY
	heavy)	GMHWVRQAPGKGLEWVAFIRYDGSNKYYADSVKGRFTISR
	construct	DNSKNTLYLQMNSLRAEDTAVYYCAKDRGLGDGTYFDYWG
		QGTTVTVSSGGSSGSSGSSHHHHHHHHGGSSGSSGSSAPT
		SSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTAMLTKKFYM
		PKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNI
		NVIVLELKGSETTFMCEYADETATIVEFLNRWITFSQSIISTLT
46	R38A,	QVQLVESGGGLVKPGGSLRLSCAASGFTFSSYGMHWVRQ	Synthesized
	F42K,	APGKGLEWVAFIRYDGSNKYYADSVKGRFTISRDNSKNTLY
	C125S IL2-	LQMNSLRAEDTAVYYCAKDRGLGDGTYFDYWGQGTTVTVS
	KYK-2	SGGGGSGGGGSGGGGSGGGGSQSALTQPASVSGSPGQSI
	(heavy-light)	TISCSGSSSNIGNNAVNWYQQLPGKAPKLLIYYDDLLPSGVS
	construct	DRFSGSKSGTSAFLAISGLQSEDEADYYCAAWDDSLNGPVF
		GGGTKLTVLGGSSGSSGSSHHHHHHHHGGSSGSSGSSAPT
		SSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTAMLTKKFYM
		PKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNI
		NVIVLELKGSETTFMCEYADETATIVEFLNRWITFSQSIISTLT
47	R38A,	GCCTTCACCGTGACTGTGCCCAAGGATCTGTACGTCGTGG	Synthesized
	F42K,	AGTACGGCTCCAACATGACAATCGAGTGCAAGTTCCCCGT
	C125S IL2-	GGAGAAGCAGCTGGACCTGGCGGCACTGATCGTGTACTG
	PDL1	GGAGATGGAGGACAAGAACATCATCCAGTTCGTTCATGGC
	construct	GAAGAGGATCTCAAGGTGCAGCACAGCAGCTACAGGCAG
		AGGGCCCGACTGCTGAAGGACCAGCTGAGCCTGGGCAAC
		GCCGCACTGCAAATCACCGACGTGAAGCTGCAGGACGCT
		GGCGTGTACAGGTGTATGATAAGCTACGGCGGAGCTGAC
		TACAAGAGAATCACGGTTAAGGTAAACGCCCCCTACGGGG
		GCAGTAGCGGAAGCTCCGGCTCAAGCCACCACCATCATC
		ATCATCACCACGGCGGCAGCAGCGGGAGCTCAGGTAGCA
		GTGGTGGGGCACCTACCTCTTCCAGCACCAAGAAGACGC
		AGCTCCAGTTGGAACACCTTCTCCTTGACCTCCAGATGAT
		CCTGAACGGCATCAACAACTACAAAAATCCCAAGCTGACC
		GCGATGCTGACGAAGAAATTCTACATGCCAAAGAAGGCCA
		CCGAGCTGAAACACCTGCAGTGTCTTGAGGAGGAACTTAA
		GCCGCTCGAGGAGGTACTGAACCTGGCCCAGAGTAAGAA
		CTTCCACCTGAGGCCCAGGGACCTCATCAGCAACATCAAT
		GTGATCGTCCTTGAGCTTAAGGGCAGCGAGACCACCTTCA
		TGTGCGAGTATGCGGACGAAACGGCCACAATCGTCGAGTT
		TCTGAATAGGTGGATCACTTTCAGCCAGAGCATCATCTCTA
		CCCTGACC
48	R38A,	AFTVTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEM	Synthesized
	F42K,	EDKNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNAALQIT
	C125S IL2-	DVKLQDAGVYRCMISYGGADYKRITVKVNAPYGGSSGSSGS
	PDL1	SHHHHHHHHGGSSGSSGSSGGAPTSSSTKKTQLQLEHLLLD
	construct	LQMILNGINNYKNPKLTAMLTKKFYMPKKATELKHLQCLEEEL
		KPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEY
		ADETATIVEFLNRWITFSQSIISTLT
49	R38A,	CTGTACATCATCGAGCACGGCAGTAACGTGACCCTGGAGT	Synthesized
	F42K,	GCAACTTCGACACCGGCAGCCACGTGAATCTGGGCGCCA
	C125S IL2-	TCACAGCTTCACTGCAGAAGGTGGAGAATGACACCTCTCC
	PDL2	CCACAGGGAGCGAGCCACCCTGCTTGAGGAACAACTGCC
	construct	TCTCGGCAAGGCCAGCTTCCACATCCCCCAGGTGCAGGT
		GAGGGACGAGGGCCAGTACCAGTGCATAATCATCTACGG
		CGTGGCCTGGGACTACAAGTACCTGACACTTAAGGTGAAA
		GCCTCCGGCGGTTCTTCCGGCTCTTCAGGCAGCTCACAC
		CATCATCATCATCACCACCATGGCGGCAGCAGCGGGAGC
		TCTGGTAGCAGTGGCGGTGCCCCCACCAGCAGTAGCACT
		AAGAAGACCCAGCTGCAACTGGAGCACTTGCTCCTGGACC
		TGCAAATGATCCTCAACGGCATCAACAACTATAAGAACCC
		CAAGCTGACGGCCATGCTGACCAAAAAGTTCTACATGCCC
		AAGAAGGCCACCGAGTTGAAACACTTGCAGTGCCTGGAG
		GAGGAGCTGAAGCCCCTGGAAGAGGTGCTGAACCTGGCC
		CAGAGCAAGAATTTTCATCTGAGGCCTAGGGACCTGATTA
		GCAACATCAACGTGATCGTGTTGGAGCTTAAAGGCTCCGA
		GACCACCTTTATGTGCGAGTACGCCGACGAGACCGCGAC
		TATCGTGGAGTTCCTGAACAGGTGGATCACCTTTTCACAG
		AGCATCATAAGCACACTGACC
50	R38A,	LYIIEHGSNVTLECNFDTGSHVNLGAITASLQKVENDTSPHRE	Synthesized
	F42K,	RATLLEEQLPLGKASFHIPQVQVRDEGQYQCIIIYGVAWDYKY
	C125S IL2-	LTLKVKASGGSSGSSGSSHHHHHHHHGGSSGSSGSSGGAP
	PDL2	TSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTAMLTKKFY
	construct	MPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISN
		INVIVLELKGSETTFMCEYADETATIVEFLNRWITFSQSIISTLT
51	PDL1	MRIFAVFIFMTYWHLLNAFTVTVPKDLYVVEYGSNMTIECKFP	Homo sapiens
		VEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRA
		RLLKDQLSLGNAALQITDVKLQDAGVYRCMISYGGADYKRIT
		VKVNAPYNKINQRILVVDPVTSEHELTCQAEGYPKAEVIWTSS
		DHQVLSGKTTTTNSKREEKLFNVTSTLRINTTTNEIFYCTFRR
		LDPEENHTAELVIPGNILNVSIKICLTLSPST
52	PDL1	MRIFAVFIFMTYWHLLNAPYNKINQRILVVDPVTSEHELTCQA	Homo sapiens
		EGYPKAEVIWTSSDHQVLSGKTTTTNSKREEKLFNVTSTLRIN
		TTTNEIFYCTFRRLDPEENHTAELVIPELPLAHPPNERTHLVIL
		GAILLCLGVALTFIFRLRKGRMMDVKKCGIQDTNSKKQSDTHL
		EET
53	PDL1	MRIFAVFIFMTYWHLLNAFTVTVPKDLYVVEYGSNMTIECKFP	Homo sapiens
		VEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRA
		RLLKDQLSLGNAALQITDVKLQDAGVYRCMISYGGADYKRIT
		VKVNAPYNKINQRILVVDPVTSEHELTCQAEGYPKAEVIWTSS
		DHQVLSGKTTTTNSKREEKLFNVTSTLRINTTTNEIFYCTFRR
		LDPEENHTAELVIPELPLAHPPNERTHLVILGAILLCLGVALTFI
		FRLRKGRMMDVKKCGIQDTNSKKQSDTHLEET
54	PDL2	IFLLLMLSLELQLHQIAALFTVTVPKELYIIEHGSNVTLECNFDT	Homo sapiens
		GSHVNLGAITASLQKVENDTSPHRERATLLEEQLPLGKASFHI
		PQVQVRDEGQYQCIIIYGVAWDYKYLTLKVKASYRKINTHILK
		VPETDEVELTCQATGYPLAEVSWPNVSVPANTSHSRTPEGL
		YQVTSVLRLKPPPGRNFSCVFWNTHVRELTLASIDLQSQMEP
		RTHPTWLLHIFIPFCIIAFIFIATVIALRKQLCQKLYSSKDTTKRP
		VTTTKREVNSAI
55	PDL2	MIFLLLMLSLELQLHQIAALFTVTVPKELYIIEHGSNVTLECNFD	Homo sapiens
		TGSHVNLGAITASLQKVENDTSPHRERATLLEEQLPLGKASF
		HIPQVQVRDEGQYQCIIIYGVAWDYKYLTLKVKASYRKINTHIL
		KVPETDEVELTCQATGYPLAEVSWPNVSVPANTSHSRTPEG
		LYQVTSVLRLKPPPGRNFSCVFWNTHVRELTLASIDLQSQME
		PRTHPTWLLHIFIPFCIIAFIFIATVIALRKQLCQKLYSSKDTTKR
		PVTTTKREVNSAVNLNLWSWEPG
56	OX40L	MERVQPLEENVGNAARPRFERNKLLLVASVIQGLGLLLCFTYI	Homo sapiens
		CLHFSTLQVSHRYPRIQSIKVQFTEYKKEKGFILTSQKEDEIM
		KVQNNSVIINCDGFYLISLKGYFSQEVNISLHYQKDEEPLFQL
		KKVRSVNSLMVASLTYKDKVYLNVTTDNTSLDDFHVNGGELI
		LIHQNPGEFCVL
57	OX40L	QVSHRYPRIQSIKVQFTEYKKEKGFILTSQKEDEIMKVQNNSV	Homo sapiens
	portion	IINCDGFYLISLKGYFSQEVNISLHYQKDEEPLFQLKKVRSVNS
		LMVASLTYKDKVYLNVTTDNTSLDDFHVNGGELILIHQNPGEF
		CVL
58	OX40L	QVSHRYPRIQSIKVQFTEYKKEKGFILTSQKEDEIMKVQNNSV	Synthesized
	construct	IINCDGFYLISLKGYFSQEVNISLHYQKDEEPLFQLKKVRSVNS
		LMVASLTYKDKVYLNVTTDNTSLDDFHVNGGELILIHQNPGEF
		CVLGGSGGGSGGGSGQVSHRYPRIQSIKVQFTEYKKEKGFIL
		TSQKEDEIMKVQNNSVIINCDGFYLISLKGYFSQEVNISLHYQ
		KDEEPLFQLKKVRSVNSLMVASLTYKDKVYLNVTTDNTSLDD
		FHVNGGELILIHQNPGEFCVLGGSGGGSGGGSGQVSHRYPR
		IQSIKVQFTEYKKEKGFILTSQKEDEIMKVQNNSVIINCDGFYLI
		SLKGYFSQEVNISLHYQKDEEPLFQLKKVRSVNSLMVASLTY
		KDKVYLNVTTDNTSLDDFHVNGGELILIHQNPGEFCVL
59	OX40L	QVSHRYPRIQSIKVQFTEYKKEKGFILTSQKEDEIMKVQNNSV	Synthesized
	N166A,	IINCDGFYLISLKGYFSQEVNISLHYQKDEEPLFQLKKVRSVNS
	F180A	LMVASLTYKDKVYLNVTTDNTSLDDFHVAGGELILIHQNPGEA
	portion	CVL
60	OX40L	QVSHRYPRIQSIKVQFTEYKKEKGFILTSQKEDEIMKVQNNSV	Synthesized
	N166A,	IINCDGFYLISLKGYFSQEVNISLHYQKDEEPLFQLKKVRSVNS
	F180A	LMVASLTYKDKVYLNVTTDNTSLDDFHVAGGELILIHQNPGEA
	construct	CVLGGSGGGSGGGSGQVSHRYPRIQSIKVQFTEYKKEKGFIL
		TSQKEDEIMKVQNNSVIINCDGFYLISLKGYFSQEVNISLHYQ
		KDEEPLFQLKKVRSVNSLMVASLTYKDKVYLNVTTDNTSLDD
		FHVAGGELILIHQNPGEACVLGGSGGGSGGGSGQVSHRYPR
		IQSIKVQFTEYKKEKGFILTSQKEDEIMKVQNNSVIINCDGFYLI
		SLKGYFSQEVNISLHYQKDEEPLFQLKKVRSVNSLMVASLTY
		KDKVYLNVTTDNTSLDDFHVNGGELILIHQNPGEFCVL
61	OX40L	QVSHRYPRIQSIKVQFTEYKKEKGFILTSQKEDEIMKVQNNSV	Synthesized
	N166A,	IINCDGFYLISLKGYFSQEVNISLHYQKDEEPLFQLKKVRSVNS
	F180A	LMVASLTYKDKVYLNVTTDNTSLDDFHVAGGELILIHQNPGEA
	construct 2	CVLGGSGGGSGGGSGQVSHRYPRIQSIKVQFTEYKKEKGFIL
		TSQKEDEIMKVQNNSVIINCDGFYLISLKGYFSQEVNISLHYQ
		KDEEPLFQLKKVRSVNSLMVASLTYKDKVYLNVTTDNTSLDD
		FHVNGGELILIHQNPGEFCVLGGSGGGSGGGSGQVSHRYPR
		IQSIKVQFTEYKKEKGFILTSQKEDEIMKVQNNSVIINCDGFYLI
		SLKGYFSQEVNISLHYQKDEEPLFQLKKVRSVNSLMVASLTY
		KDKVYLNVTTDNTSLDDFHVNGGELILIHQNPGEFCVL
62	OMCP-	HKLAFNFNLEINGSDTHSTVDVYLDDSQIITFDGKDIRPTIPFMI	Synthesized
	OX40L	GDEIFLPFYKNVFSEFFSLFRRVPTSTPYEDLTYFYECDYTDN
	construct	KSTFDQFYLYNGEEYTVKTQEATNKNMWLTTSEFRLKKWFD
		GEDCIMHLRSLVRKMEDSKRNTGGGSSGSSGSSHHHHHHH
		HGGSSGSSGSSGGQVSHRYPRIQSIKVQFTEYKKEKGFILTS
		QKEDEIMKVQNNSVIINCDGFYLISLKGYFSQEVNISLHYQKD
		EEPLFQLKKVRSVNSLMVASLTYKDKVYLNVTTDNTSLDDFH
		VNGGELILIHQNPGEFCVLGGSGGGSGGGSGQVSHRYPRIQ
		SIKVQFTEYKKEKGFILTSQKEDEIMKVQNNSVIINCDGFYLISL
		KGYFSQEVNISLHYQKDEEPLFQLKKVRSVNSLMVASLTYKD
		KVYLNVTTDNTSLDDFHVNGGELILIHQNPGEFCVLGGSGGG
		SGGGSGQVSHRYPRIQSIKVQFTEYKKEKGFILTSQKEDEIM
		KVQNNSVIINCDGFYLISLKGYFSQEVNISLHYQKDEEPLFQL
		KKVRSVNSLMVASLTYKDKVYLNVTTDNTSLDDFHVNGGELI
		LIHQNPGEFCVL
63	OMCP-	HKLAFNFNLEINGSDTHSTVDVYLDDSQIITFDGKDIRPTIPFMI	Synthesized
	OX40L	GDEIFLPFYKNVFSEFFSLFRRVPTSTPYEDLTYFYECDYTDN
	N166A,	KSTFDQFYLYNGEEYTVKTQEATNKNMWLTTSEFRLKKWFD
	F180A	GEDCIMHLRSLVRKMEDSKRNTGGGSSGSSGSSHHHHHHH
	construct	HGGSSGSSGSSGGQVSHRYPRIQSIKVQFTEYKKEKGFILTS
		QKEDEIMKVQNNSVIINCDGFYLISLKGYFSQEVNISLHYQKD
		EEPLFQLKKVRSVNSLMVASLTYKDKVYLNVTTDNTSLDDFH
		VAGGELILIHQNPGEACVLGGSGGGSGGGSGQVSHRYPRIQ
		SIKVQFTEYKKEKGFILTSQKEDEIMKVQNNSVIINCDGFYLISL
		KGYFSQEVNISLHYQKDEEPLFQLKKVRSVNSLMVASLTYKD
		KVYLNVTTDNTSLDDFHVAGGELILIHQNPGEACVLGGSGGG
		SGGGSGQVSHRYPRIQSIKVQFTEYKKEKGFILTSQKEDEIM
		KVQNNSVIINCDGFYLISLKGYFSQEVNISLHYQKDEEPLFQL
		KKVRSVNSLMVASLTYKDKVYLNVTTDNTSLDDFHVNGGELI
		LIHQNPGEFCVL
64	OMCP-	HKLAFNFNLEINGSDTHSTVDVYLDDSQIITFDGKDIRPTIPFMI	Synthesized
	OX40L	GDEIFLPFYKNVFSEFFSLFRRVPTSTPYEDLTYFYECDYTDN
	N166A,	KSTFDQFYLYNGEEYTVKTQEATNKNMWLTTSEFRLKKWFD
	F180A	GEDCIMHLRSLVRKMEDSKRNTGGGSSGSSGSSHHHHHHH
	construct 2	HGGSSGSSGSSGGQVSHRYPRIQSIKVQFTEYKKEKGFILTS
		QKEDEIMKVQNNSVIINCDGFYLISLKGYFSQEVNISLHYQKD
		EEPLFQLKKVRSVNSLMVASLTYKDKVYLNVTTDNTSLDDFH
		VAGGELILIHQNPGEACVLGGSGGGSGGGSGQVSHRYPRIQ
		SIKVQFTEYKKEKGFILTSQKEDEIMKVQNNSVIINCDGFYLISL
		KGYFSQEVNISLHYQKDEEPLFQLKKVRSVNSLMVASLTYKD
		KVYLNVTTDNTSLDDFHVNGGELILIHQNPGEFCVLGGSGGG
		SGGGSGQVSHRYPRIQSIKVQFTEYKKEKGFILTSQKEDEIM
		KVQNNSVIINCDGFYLISLKGYFSQEVNISLHYQKDEEPLFQL
		KKVRSVNSLMVASLTYKDKVYLNVTTDNTSLDDFHVNGGELI
		LIHQNPGEFCVL
65	4-1BBL	ACPWAVSGARASPGSAASPRLREGPELSPDDPAGLLDLRQ	Homo sapiens
	portion	GMFAQLVAQNVLLIDGPLSWYSDPGLAGVSLTGGLSYKEDT
		KELVVAKAGVYYVFFQLELRRVVAGEGSGSVSLALHLQPLRS
		AAGAAALALTVDLPPASSEARNSAFGFQGRLLHLSAGQRLG
		VHLHTEARARHAWQLTQGATVLGLFRVTPEIPAGLPSPRSE
66	4-1BBL	ACPWAVSGARASPGSAASPRLREGPELSPDDPAGLLDLRQ	Synthesized
	construct	GMFAQLVAQNVLLIDGPLSWYSDPGLAGVSLTGGLSYKEDT
		KELVVAKAGVYYVFFQLELRRVVAGEGSGSVSLALHLQPLRS
		AAGAAALALTVDLPPASSEARNSAFGFQGRLLHLSAGQRLG
		VHLHTEARARHAWQLTQGATVLGLFRVTPEIPAGLPSPRSEG
		GSGGGSGGGSGACPWAVSGARASPGSAASPRLREGPELS
		PDDPAGLLDLRQGMFAQLVAQNVLLIDGPLSWYSDPGLAGV
		SLTGGLSYKEDTKELVVAKAGVYYVFFQLELRRVVAGEGSG
		SVSLALHLQPLRSAAGAAALALTVDLPPASSEARNSAFGFQG
		RLLHLSAGQRLGVHLHTEARARHAWQLTQGATVLGLFRVTP
		EIPAGLPSPRSEGGSGGGSGGGSGACPWAVSGARASPGSA
		ASPRLREGPELSPDDPAGLLDLRQGMFAQLVAQNVLLIDGPL
		SWYSDPGLAGVSLTGGLSYKEDTKELVVAKAGVYYVFFQLE
		LRRVVAGEGSGSVSLALHLQPLRSAAGAAALALTVDLPPASS
		EARNSAFGFQGRLLHLSAGQRLGVHLHTEARARHAWQLTQ
		GATVLGLFRVTPEIPAGLPSPRSE
67	OMCP-	HKLAFNFNLEINGSDTHSTVDVYLDDSQIITFDGKDIRPTIPFMI	Synthesized
	41BBL	GDEIFLPFYKNVFSEFFSLFRRVPTSTPYEDLTYFYECDYTDN
	construct	KSTFDQFYLYNGEEYTVKTQEATNKNMWLTTSEFRLKKWFD
		GEDCIMHLRSLVRKMEDSKRNTGGGSSGSSGSSHHHHHHH
		HGGSSGSSGSSGGACPWAVSGARASPGSAASPRLREGPEL
		SPDDPAGLLDLRQGMFAQLVAQNVLLIDGPLSWYSDPGLAG
		VSLTGGLSYKEDTKELVVAKAGVYYVFFQLELRRVVAGEGS
		GSVSLALHLQPLRSAAGAAALALTVDLPPASSEARNSAFGFQ
		GRLLHLSAGQRLGVHLHTEARARHAWQLTQGATVLGLFRVT
		PEIPAGLPSPRSEGGSGGGSGGGSGACPWAVSGARASPGS
		AASPRLREGPELSPDDPAGLLDLRQGMFAQLVAQNVLLIDGP
		LSWYSDPGLAGVSLTGGLSYKEDTKELVVAKAGVYYVFFQL
		ELRRVVAGEGSGSVSLALHLQPLRSAAGAAALALTVDLPPAS
		SEARNSAFGFQGRLLHLSAGQRLGVHLHTEARARHAWQLT
		QGATVLGLFRVTPEIPAGLPSPRSEGGSGGGSGGGSGACP
		WAVSGARASPGSAASPRLREGPELSPDDPAGLLDLRQGMF
		AQLVAQNVLLIDGPLSWYSDPGLAGVSLTGGLSYKEDTKELV
		VAKAGVYYVFFQLELRRVVAGEGSGSVSLALHLQPLRSAAG
		AAALALTVDLPPASSEARNSAFGFQGRLLHLSAGQRLGVHLH
		TEARARHAWQLTQGATVLGLFRVTPEIPAGLPSPRSE

EXAMPLES

The following examples are included to demonstrate preferred embodiments of the invention. It should be appreciated by those of skill in the art that the techniques disclosed in the examples that follow represent techniques discovered by the inventors to function well in the practice of the invention, and thus can be considered to constitute preferred modes for its practice. However, those of skill in the art should, in light of the present disclosure, appreciate that many changes can be made in the specific embodiments which are disclosed and still obtain a like or similar result without departing from the spirit and scope of the invention.

Introduction to Examples 1-6

The IL2Rα chain serves to capture IL2 at the cell surface to facilitate subsequent binding to the signaling part of the receptor, namely the IL2Rβγ chains. Resting cytotoxic lymphocytes, such as natural killer (NK) and CD8⁺ T cells, do not express appreciable IL2Rα at the cell surface and are thus not activated by low levels of IL2¹. IL2Rα is expressed on this population after initial activation, however, and is required for maximum cytotoxic lymphocyte expansion². High dose IL2 can induce the activation of all cytotoxic I sr,lofQW2/GV A/ymphocytes and is approved for treatment of several malignancies with an approximately 15% partial or complete tumor response^3-5. Most patients do not benefit from such therapy due to activation of regulatory T cell (T_regs) and complications such as severe blood pressure alteration, generalized capillary leak, and end organ failure due to activation of vascular endothelium^{6, 3, 7}. Both vascular endothelium and T_regs express IL2Rα and are thus preferentially activated by IL2 over cytotoxic lymphocytes⁸. Lowering the IL2 dose can ameliorate side effects but also decreases efficacy. Mutant forms of IL2, such as those with substitutions of alanine for arginine at the 38 position (R38A) and/or lysine for phenylalanine at the 42 position (F42K), decrease the affinity of IL2 for IL2Rα and thus eliminate many side effects⁹. Such IL2a mutants may also decrease the efficacy of immunotherapy². A form of IL2 that could preferentially activate cytotoxic lymphocytes in the absence of IL2Rα reactivity would be highly advantageous for clinical applications.

NKG2D recognizes MHC class-I-related stress ligands expressed by malignant or virally-transformed cells¹⁰. Of all the activating immunoreceptors NKG2D has the highest specificity for cytotoxic lymphocytes as it is constitutively expressed on both murine and human NK cells as well as activated CD8⁺ T cells¹¹. Consequentially it has been argued that tumors and virally infected cells utilize shed NKG2D ligands as a mechanism of immune evasion^{12, 13}. Orthopox major histocompatibility complex class I-like protein, or OMCP, is an NKG2D ligand decoy shed by monkeypox and cowpox virus infected cells. It is not expressed by small pox or vaccinia virus and thus not recognized by those immunized with small pox vaccine. As OMCP binds to both human and murine NKG2D with the highest affinity of any known ligand we thought it might function as an ideal targeting vector to optimally deliver IL2 to cytotoxic lymphocytes^{14, 15}. Here we describe the construction and function of a fusion protein designed to deliver an IL2Rα mutant to NKG2D-expressing lymphocytes¹⁵. We demonstrate that this construct overcomes decreased efficacy associated with mutations in the IL2Rα binding region while retaining a favorable safety profile. Systemic administration of this fusion protein improves immunotherapy against both solid and liquid tumors. Targeted delivery of IL2 can thus be safely used to maximally activate NKG2D-expressing lymphocytes, such as NK cells, to optimize immunotherapy without systemic side effects.

Example 1. NKG2D-Targeted Delivery of an IL2 Mutant Preferentially Activates Cytotoxic Lymphocytes In Vitro

To overcome the preferential activation of IL2Rα-expressing cells, we designed an IL2 fusion protein that would target cytotoxic lymphocytes directly via the NKG2D receptor. This fusion protein combines the high affinity NKG2D ligand OMCP with an IL2 mutated to reduce IL2Rα reactivity. Our construct, termed OMCP-mutIL2, consists of the 152 residue OMCP protein fused to the N-terminus of the 133 amino acid R38A/F42K mutant form of human IL2 (mutIL2) via a flexible 30 residue linker (FIG. 1A-B). The construct was first assessed for its in vitro binding ability. Binding of fluorescently labeled construct was tested in vitro at 37° C. in bulk splenocytes. FIG. 17 shows that the construct appears to only bind to NK cells which express NKG2D. The construct does not show binding to CD4+CD3+ T cells, CD8⁺ CD3+ T cells, CD11C+CD11b− DCs, CD11c−CD11b+ Macs or CD19+CD3− B cells.

We have previously demonstrated strain-specific differences in murine NK cell cytotoxicity and lung cancer immunosurveillance¹⁶ (and Example 7). Therefore, we set out to examine the efficacy of OMCP-mut-IL2 in activation of NK cells from two different strains of mice, namely A/J and B6 with poor and robust NK function, respectively. Compared to wild-type IL2 (wtIL2) or mutIL2, OMCP-mutIL2 strongly upregulated CD69 on NK cells of both strains after 36-hour co-culture with 100 IUe/ml of cytokine (FIG. 1C, left; FIG. 6 , left two graphs)^{16, 17}. At high concentrations a similar increase in CD69 expression was observed with OMCP-mut-IL2, wtlL2 or mutIL2 (FIG. 6 ). Activation of CD4⁺Foxp3⁺ T_regs, as measured by upregulation of ICOS, was evident with wtlL2 only, but not with mutIL2 or OMCP-mutIL2 (FIG. 1C-D). CD8⁺ and CD4⁺Foxp3⁻ effector T cells, on the other hand, demonstrated no upregulation of CD69 after 36 hours, even at highest doses of cytokines (FIG. 1C-D and data not shown). Longer exposure over a period of five days led to proliferation of both NK and CD8⁺ T cells exposed to wtlL2 and OMCP-mutIL2 (FIG. 1E-F). Importantly, OMCP-mutIL2 activated CD8⁺ T cells and NK cells equivalently to mutIL2 in NKG2D^−/− splenocytes, indicating that the increased activation was due to the effect of OMCP targeting upon NKG2D-bearing cells (FIG. 1F; FIG. 6 , right two graphs). Only incubation with wtlL2 led to CD4⁺Foxp3⁺ T_regs and CD4⁺Foxp3⁻ effector cell proliferation (FIG. 1E-F). Thus exposure to OMCP-mutIL2 results in preferential NK activation that is superior or equivalent to wtlL2 in a dose-dependent manner. CD8⁺ T cells can also be activated but require prolonged exposure to higher doses of OMCP-mutIL2.

Example 2. Low-Dose Cytokine Therapy Offers a Favorable Safety Profile

Dose-dependent toxicity can limit cytokine administration in vivo. To model human immunotherapy protocols we next treated NJ mice with wtlL2 given as ten doses over a five day cycle¹⁸. While A/J mice tolerated 750,000 IUe of wtlL2, significant mortality was evident at higher doses (FIG. 2A-B). Even after a 750,000 IUe dose mice demonstrated extreme distress, weight loss, decreased food consumption, ascites and hepatic inflammation (FIG. 2A-E; FIG. 7A-C). These side-effects mirror the capillary leak and distress associated with high dose IL2 therapy in humans⁷. Treatment with anti-Asialo-GM1 ameliorated mortality, but not weight loss, induced by high dose wtlL2 (1,500,000 IUe) in A/J mice, confirming that side effects of such therapy can occur independent of NK cells (FIG. 2F-K). Unlike the case for wtlL2 no animal death was evident after 1,500,000 IUe of OMCP-mutIL2 or mutIL2 in the presence or absence of NK cells. Animal weight loss after 1,500,000 IUe of OMCP-mutIL2 occurred only in NK-sufficient mice suggesting that toxicity of our construct was solely due to immunoactivation (FIG. 2F-K). A regimen of 200,000 IUe was well tolerated in A/J mice with minimal weight loss, distress, or organ inflammation for all cytokines (FIG. 2L-O). Capillary leak, however, was still evident by accumulation of pleural effusion and ascites after wtIL2, but not OMCP-mutIL2 or mutIL2, at this dose. B6 mice were able to tolerate higher doses of wtIL2 but still suffered significant morbidity over 750,000 IUe (FIG. 7D).

Example 3. OMCP-mutIL2 Preferentially Expands and Activates NK Cells In Vivo Compared to wtIL2 or mutIL2

To evaluate immunologic changes associated with cytokine treatment, NJ mice received 200,000 IUe of cytokine or construct given as ten equal doses over five days. Splenic lymphocytes were evaluated flow cytometrically on day six. Both wtIL2 and OMCP-mutIL2 increased lymphocyte content and splenic size over saline-treated controls (FIG. 3A-B). OMCP-mutIL2 led to a substantial expansion and activation of NK cells measured by cellularity and surface KLRG1 levels (FIG. 3C). In OMCP-mutIL2 treated mice NK cells comprised close to half of all splenic lymphocytes, paralleling or even surpassing the total lymphocyte counts of saline or mutIL2-treated mice (FIG. 3A vs. FIG. 3C). NK expansion by 200,000 IUe of OMCP-mutIL2 was superior to near toxic doses of wtIL2 (750,000 IU), high dose mutIL2 (3,500,000 IUe), or wtIL2 complexed to anti-IL2 antibody (clone MA6602)¹⁹ (FIG. 3C). In fact, the majority of mice could not tolerate the full 200,000 IUe of wtIL2/anti-IL2 antibody and injections had to be terminated at 160,000 or 180,000 IUe with requisite animal sacrifice due to animal distress and rapid weight loss (FIG. 8A). WtIL2 led to a significant expansion of CD4⁺Foxp3⁺ T_regs, specifically the ICOS⁺ subset⁶ in NJ mice even when complexed to anti-IL2 antibodies (FIG. 3D). Importantly the NK/T_reg ratio, which has been described as a predictive factor for success of immunotherapy²⁰, was dramatically increased in OMCP-mutIL2 treated mice compared to all other treatment conditions (FIG. 3E). Superior expansion of NK cells by OMCP-mutIL2 was even possible at doses 2-fold lower than wtIL2 (FIG. 8B). However, targeting NKG2D with a ˜500-fold lower affinity NKG2D ligand, ULBP3, ameliorated efficacy of the fusion construct for expansion but still offered superior NK activation compared to mutIL2 alone (FIG. 8B). No statistically significant increase in CD4⁺Foxp3⁻ or CD8⁺ T lymphocytes was evident after wtIL2 or OMCP-mutIL2 treatment, although a trend for CD8⁺ T cell expansion was evident (FIG. 8C-D). Such data is consistent with the prevalence of naïve T lymphocytes, expressing low levels of IL2 receptors and NKG2D in specific pathogen-free mice.

Unlike the A/J strain little immunoactivation of lymphocytes was evident in B6 mice treated with 200,000 IUe of wtIL2 (data not shown). At higher doses of 750,000 IUe OMCP-mutIL2 expanded NK cells more robustly than wtIL2 in this strain (FIG. 3F-H). IL2/anti-IL2 antibody complexes prevented T_reg expansion but, similar to the A/J strain, such treatment had toxicity and the majority of B6 mice could not tolerate the full 750,000 IUe dose (FIG. 3I). OMCP-mutIL2, however, was well tolerated at this dose and led to a high NK/T_reg ratio (FIG. 3J). No expansion of NK cells was evident in OMCP-mutIL2 treated B6 NKG2D^−/− mutants, confirming the requirement for NKG2D in the function of our construct (data not shown). No statistically significant expansion of B6 CD8⁺ or CD4⁺Foxp3⁻ T cells was evident in any treatment group although a trend for CD8⁺ T cell expansion was evident after wtIL2 administration (FIG. 8F-G). Identical data was obtained for lung resident lymphocytes in both the NJ and B6 strains (data not shown).

Example 4. OMCP-mutIL2 Preferentially Expands and Activates NK Cells in Human Peripheral Blood Lymphocytes Compared to wtIL2 or mutIL2

To demonstrate the effectiveness of OMCP-mutIL2 in human lymphocytes, human peripheral blood lymphocytes were co-cultured for 36 hours in 100 IUe of either wild-type IL2, R38A/F42K mutant form of IL2 or OMCP-mutant IL2.

NK Cells:

The cells were flow cytometrically analyzed and relative prevalence of CD56+CD3− NK cells compared between conditions. A relatively higher proportion of NK cells was evident in the OMCP-mutant IL2 group (FIG. 31A). Perforin levels were higher in OMCP-mutant IL2 treated NK cells (red) compared to saline (black), IL2 (blue) or mutant IL2 (green) treated ones (FIG. 31B).

CD8+ T Cells:

Similar to NK cells, higher intracellular levels of perforin were evident in CD8+ T cells treated with OMCP-mutant IL2 compared to other conditions (FIG. 31C).

Tregs:

When gating on CD4⁺Foxp3+CD45RA− T cells a relatively higher proportion of activated CD25+CD127− regulatory T cells was evident in IL2 treated peripheral blood lymphocyte cultures compared to other conditions (FIG. 31D). Taken together this data suggests that OMCP-mutIL2 preferentially expands and activates NK cells and CD8+ cells in human peripheral blood lymphocytes compared to wtIL2 or mutIL2. Importantly, OMCP-mutIL2 does not activated regulatory T cells significantly relative to IL2.

Example 5. Treatment with OMCP-mutIL2 Offers Superior Immunologic Control of Malignancies In Vivo

Unlike T lymphocytes, which require prior antigen encounter for optimal antigen-specific tumor cytotoxicity, NK cells can mediate natural cytotoxicity without prior sensitization. NK cells also form the primary barrier for expansion of select malignancies, such as lymphoma and lung cancer^{16, 17, 21, 22}. Treatment of NJ mice with OMCP-mutIL2, compared to wtIL2 or mutIL2, led to enhanced in vivo clearance and in vitro lysis of YAC-1 cells by bulk splenocytes (FIG. 4A, FIG. 9A-B). Decreased growth of the highly aggressive Lewis Lung Carcinoma (LLC) cell line was evident in B6 mice after 750,000 IUe of OMCP-mutIL2 compared to wtIL2 or mutIL2. Increased cytotoxicity was evident in OMCP-mutIL2 treated splenocytes for the LLC cell line as well (FIG. 4B-C; FIG. 9A-C). Enhanced immunotherapy was lost in NKG2D^−/− mice or following NK depletion (FIG. 4D-E). In the absence of host NKG2D mutIL2 actually increased the rate of LLC growth. Thus OMCP-mediated targeting of mutIL2 offers a safer and more efficacious form of immunotherapy for both solid and liquid tumors in various strains of mice.

Example 6. Impact of NKG2D Targeting on IL2 Signaling

Antibody-IL2 conjugates, or IL2/anti-IL2 antibody complexes demonstrate improved biologic activity over purified cytokine by extending the duration of serum half-life^{23, 24}. To investigate whether linking IL2 to OMCP increased serum half-life, we injected 500,000 IUe of fluorescently-labeled wtIL2, mutIL2 or OMCP-mutIL2 into A/J and B6 mice and monitored serum clearance by serial blood draws. While OMCP-mutIL2 had a slightly higher serum concentration at early time points, all constructs were undetectable in the blood one hour post-injection (FIG. 5A-B). This is significantly shorter than the described 11-14 hour serum half-life of antibody-IL2 conjugates²³. Interestingly, despite the injection of identical amount of cytokine, lower cytokine levels were detected in B6 mice compared to A/J mice at all time points. Such data points to strain-specific differences in clearance of IL2 and may explain why B6 mice are able to both tolerate and require higher doses of cytokine for NK expansion. Nevertheless, based on this data it is unlikely that prolonged circulation of construct was responsible for the increased activity of OMCP-mutIL2 over wtIL2.

We next considered the possibility that the superiority of OMCP-mutIL2 was the result of signaling through NKG2D as antibody-mediated crosslinking of this receptor can activate NK cells (FIG. 10A)²⁵. While the addition of purified OMCP to mutIL2 did not augment NK activation or expansion in vitro or in vivo (data not shown) we would not expect a monomeric ligand to crosslink NKG2D. We thus directly compared NK cell activation in the presence of 1000 IUe of OMCP-mutIL2, mutIL2 and mutIL2 combined with equimolar concentration of pentamerized OMCP. No increase in NK activation, as measured by CD69 upregulation or degranulation, was evident in the presence of pentamerized OMCP (FIG. 5C, FIG. 10B). This suggests that NKG2D crosslinking is not responsible for augmented NK cell activation by OMCP-mutIL2 at physiologic concentrations.

To evaluate IL2 signaling we next quantitated STAT5 phosphorylation after a 15 minute cytokine stimulation of freshly isolated NK cells in vitro. Lower levels of STAT5 phosphorylation were evident in NJ compared to B6 NK cells at all concentrations tested (FIG. 5D-E) suggesting that lymphocyte dysfunction of NJ mice may at least partially be the result of inefficient IL2 signal transduction. Surprisingly, for both B6 and A/J NK cells wtIL2 and OMCP-mutIL2 demonstrated an identical dose-dependent pattern of STAT5 phosphorylation (FIG. 5D-E). In the absence of NKG2D reactivity OMCP-mutIL2 failed to increase STAT5 phosphorylation over mutIL2 alone. Taken together these data suggested that IL2a reactivity is important for peak IL2 signaling in resting NK cells, and that NKG2D-binding may effectively substitute for IL2Rα-binding in IL2-mediated signal transduction. Such data, however, failed to explain the superior NK activation by OMCP-mutIL2 in vivo or in bulk splenocyte cultures (FIG. 1C-D, FIG. 3 ).

IL2 signaling results in the internalization of IL2/IL2R, with subsequent degradation of IL2 and IL2Rβγ. The binding of OMCP-mutIL2 to both the IL2 receptor and NKG2D could thus lead to altered internalization and enhanced NK cell activation by prolonging IL2 signaling. To test this we stimulated freshly isolated NK cells for 15 minutes, replaced the culture media with cytokine free media, and monitored STAT5 phosphorylation for four hours. Identical decay of phospho-STAT5 was evident for both wtIL2 and OMCP-mutIL2 (FIG. 5F-G). Thus altering duration of IL2 signaling is not responsible for superior NK activation by OMCP-mutIL2.

We next considered the possibility that superior NK activation by OMCP-mutIL2 may be the result of altered cytokine interaction with competing stromal cells (FIG. 5H). Indeed, in the presence of other splenocytes OMCP-mutIL2 demonstrated a dose-dependent enhancement in NK STAT5 phosphorylation over wtIL2 (FIG. 5I). We next explored the interplay between IL2Rα expression by stromal cells and NKG2D expression by NK cells on IL2 signal transduction. To accomplish this we isolated splenic NK cells from either wild-type or NKG2D^−/− B6 mice and combined them with wild-type splenocytes depleted of NK cells. Cultures were recombined in a 1:20 NK:splenocyte ratio, resembling the proportion normally present in resting wild-type B6 mice. For some cultures NK cell depleted splenocytes were treated with saturating concentrations of IL2Rα-blocking antibody (clone 3C7) prior to recombining with wild-type NK cells. The cultures were then stimulated with 1000 IUe of either wtIL2 or OMCP-mutIL2 for 15 minutes. STAT5 phosphorylation was identical in NKG2D^−/− or wild type NK cells in the presence of wtIL2 (FIG. 5J, left two columns). Wild-type NK cells cultured with OMCP-mutIL2 demonstrated superior STAT5 phosphorylation to cultures with wtIL2. Little STAT5 phosphorylation was evident in NKG2D^−/− NK cells cultured with OMCP-mutIL2 (FIG. 5J, right two columns). In the presence of IL2Rα-blockade of competing splenocyte stromal cells, NK cell STAT5 phosphorylation by wtIL2 increased to levels comparable to OMCP-mutIL2 (FIG. 5K). Taken together these data demonstrate that IL2-Ra expression by “competing” stromal cells limits NK cell activation by wtIL2 and this competition can be eliminated by the NKG2D-targeted, IL2Rα-binding impaired OMCP-mutIL2 construct.

Discussion for Examples 1-6

While IL2 therapy initially showed great promise, it has been limited by activation of T_regs and toxic side effects associated with activation of vascular endothelium. Several strategies have been proposed to preferentially activate cytotoxic lymphocytes. One strategy has been to create mutants with increased affinity for IL2Rβ to remove the preference for IL2Rα^{26, 27}. Importantly, these IL2 mutants retain wild type binding for IL2Rα, and would therefore still be recognized by T_reg cells and vascular endothelium. Our results also suggest that competition with IL2-Rα⁺-expressing cells limits bioavailability of wtIL2 to cytotoxic lymphocytes.

Another promising therapy involves anti-IL2 antibodies that sterically inhibit wtIL2 binding to IL2Rα^{1, 28, 29}. Such treatment can extend serum half-life²⁴ due to the Fc region of the antibody and potentially due to reduced competition for wtIL2 from IL2Rα-expressing cells. Antibody-IL2 fusion proteins have also been designed to target IL2 to specific tumor antigens^{30, 31}. While offering the potential for personalized therapy such antibody-mediated delivery of IL2 to the tumor depends on the expression of a known tumor associated antigen, a situation that often does not exist. This approach could potentially be further limited by tumor-mediated alteration of the targeted antigen.

Finally, IL2 mutants with reduced affinity for IL2Rα have been tested extensively. Compared to wtIL2 these mutants can be administered in supratherapeutic doses without IL2Rα-mediated capillary leak or systemic toxicity³². While these mutants have excellent safety profiles, they activate cytotoxic lymphocytes poorly (FIG. 5C-E)³³. Our approach combines several of the concepts above to target a safe form of IL2 directly to cytotoxic lymphocytes, instead of tumors. This is accomplished by replacing the normal targeting of IL2 to IL2Rα with NKG2D. The combination of an IL2Rα-deficient IL2 fused to a high affinity NKG2D-ligand improves upon previous strategies by specifically expanding NK cells without any apparent activation of T_regs or capillary leak. These findings offer the promise of a potentially safe and highly efficacious form of IL2.

One limitation in translating results from inbred lab animals to humans is the natural diversity in cytokine reactivity and environmentally dependent threshold for lymphocyte activation. Previous studies have demonstrated a correlation between ex vivo killing of tumor cells and enhanced long-term cancer immunity³⁴. Therefore, any potential therapy needs to account for a population that has differential levels of cytotoxic lymphocyte activity. We have thus attempted to model this natural variation by using two strains of mice known to be highly resistant (B6) or susceptible (NJ) to carcinogenesis. For example, NK cells from B6 mice, are activated by wtIL2 and extreme doses of mutIL2. In contrast, IL2/anti-IL2 antibody complexes resulted in expansion of NK cells in NJ but not in B6 mice. Such variations highlight the limitations of translating results derived from a single strain of mice to immunologically diverse humans. Importantly, the OMCP-mutIL2 construct was able to expand NK cells in both strains of mice, indicating that this therapy could be efficacious in populations with diverse NK function and cytokine reactivity.

Since OMCP has been described as an evolutionary antagonist of NKG2D³⁵ blockade of this immunoreceptor at the time of tumor therapy may be construed as counterproductive. Nevertheless, natural cytotoxicity and tumor clearance was augmented in OMCP-mutIL2-treated mice even in the presence of established tumors. This suggests minimal or transient NKG2D receptor occupancy and preservation of function. Alternatively recent reports have demonstrated that shed NKG2D ligands may actually promote tumor immunity through reversal of NK desensitization imposed by chronic agonistic engagement³⁶. While we did not detect NK activation or expansion by monomeric or even pentameric OMCP, it is possible that within the tumor bed such competitive antagonism plays a paradoxical role in NK activation. In addition, IL2 may upregulate receptors necessary for NK migration and tumor infiltration. It is thus possible that anti-tumor immunity mediated by OMCP-mutIL2 may depend on NK cells located outside the tumor bed and not subject to local tumor-specific tolerance or anergy. Furthermore, OMCP may be the ideal “targeting vector” due to its high affinity and long half-life of binding to human NKG2D.

While NK cells from two separate strains of mice were activated by OMCP-mutIL2 we did not detect global expansion of activation of CD8⁺ T cells by our construct. This is most likely due to the fact that NKG2D is expressed only on select subsets of CD8⁺ T cells, namely memory or activated cytotoxic lymphocytes. Based on the paucity of this cell population in mice raised in specific pathogen-free environment, OMCP-mutIL2-mediated activation was limited in our system to NK cells. To this end we focused on immunotherapy for lung cancer and lymphoma, whose growth is regulated primarily by NK cells^{16, 17, 22, 37}. Nevertheless OMCP-mutIL2 was able to expand CD8⁺ T cells when administered in high concentrations in vitro (FIG. 1E-F). Thus, it may be possible that NKG2D-targeted delivery of immunostimulatory cytokines may lead to the expansion and/or activation of antigen-specific CD8⁺ memory cells for long-term tumor immunity under normal immunologic conditions.

Methods for Examples 1-6

Cytokine and Construct Generation:

The sequences encoding human IL2 (1-133; C125S) and mutant IL2 (1-133; R38A, F42K, C125S) were cloned into the pFM1.2R³⁸ with an N-terminal FLAG/hexahistidine tag. The chimeric OMCP-mutIL2 molecule comprises the full-length OMCP (1-152) coding sequence cloned in frame with a C-terminal FLAG/hexahistidine tag-mutant IL2 (1-133; R38A, F42k, C125S) cloned into the pFM1.2R vector. Proteins were expressed by transient transfection into HEK293F (Life Technologies). Supernatant was recovered at 72 h and 144 h post-transfection. Supernatants were supplemented with 5 mM imidazole and 0.02% sodium azide and purified by nickel-nitrilotriacetic acid (Ni-NTA) chromatography (Qiagen). Purified proteins were buffer exchanged into saline and flash frozen in liquid nitrogen. Equivalent in vitro and in vivo activity was documented for wild-type IL2 generated in house and Teceleukin (Tecin™) available from the NCI repository (Frederick National Laboratory for Cancer Research). Thus for some experiments these two preparations of IL2 were used interchangeably.

Wild-type IL2 has a specific activity of 15×10⁶ IU/mg³⁹. Thus, based on the molecular weight of 15.5 kDa a 4.4 μM solution is equivalent to 1000 Based on this calculation all cytokines and construct were administered on a molar basis with 1 μl of 4.4 μM solution defined as 1000 IU equivalents (IUe from here on). Such a system allows for equimolar comparison between IL2, mutIL2 and OMCP-mutIL2 despite difference in molecular weight.

Animals:

NJ (8-12 weeks) and C57BL/6J (6-9 weeks) strains of mice were purchased from the Jackson Laboratory (Bar Harbor, Me.). NKG2D^−/− mice on the B6 background were kindly provided by Wayne Yokoyama and bred in house (Howard Hughes Institute of Medicine at Washington University in St. Louis). Animals were housed in a barrier facility in air-filtered cages and allowed free access to food and water. For some experiments NJ mice were treated with depleting concentrations of anti-Asialo-GM1 (50 μl day −2; 25 μl day −1) or control rabbit IgG (Wako Chemical Company). Animal procedures were approved by the animal studies committee of Washington University School of Medicine, St. Louis, Mo.

Tissue Harvest and In Vitro Cultures:

Single cell suspension of splenocytes were obtained by crushing whole spleens through 70 μm cell strainers prior to RBC lysis by ACK buffer (Lonza, Walkersville, Md.) and re-filtration through a 40 μm filter. Lungs were digested for 90 minutes at 37° C. in 1 mg/ml collagenase II (Fisher Scientific), and 5 U/ml DNase I (Sigma-Aldridge) prior to processing in an identical fashion to spleens.

For in vitro cultures splenocytes from either A/J, B6, or NKG2D^−/− mice were extracted in a sterile fashion and seeded in 12-well plates in complete media (RPMI 1640 supplemented with 10% FBS, 100 U/ml Penicillin and Streptomycin, 2 mM L-glutamine and 50 μM 2-Mercaptoethanol) at 5 million cells per ml per well. The cells were treated with increasing doses of human recombinant IL2, mutIL2, OMCP-mutIL2, or OMCP for 36 hours as described in the manuscript. For some experiments bulk splenocytes were labeled with CFSE and cultured in 1000 IUe/ml of cytokine for 5 days prior to flow cytometric analysis. For NK isolation experiments bulk splenocytes were processed using either the NK cell isolation kit II or CD49b (DX5) positive magnetic bead selection (both from Miltenyi Biotech). For STAT5 phosphorylation experiments, isolated NK cells were stimulated in increasing concentrations of IL2 or construct at 100,000 cells/500 μl for 15 minutes. For experiments evaluating the interaction of NK cells with splenic stroma, DX5 positively selected NK cells were labeled with CFSE (for identification after fixation and permeabilization) and recombined with NK depleted stromal cells. As described in the manuscript, for some studies NKG2D^−/− NK cells were combined with wild-type splenocyte stromal cells. For other experiments, NK-depleted splenocytes from wild-type B6 mice were treated with saturating concentrations of anti-IL2a blocking antibody (clone 3C7) or isotype control (both from Biolegend) prior to recombining with NK cells. For such competitive STAT5 phosphorylation experiments 100,000 cells were resuspended into 2 μl complete media containing 1,000 IU/ml of either wtIL2, mutIL2 or OMCP-mut-IL2 (freshly prepared and pre-warmed). The cells were then incubated at 37° C. for 15 minutes

Flow Cytometry:

All flow cytometric analysis was performed using saturating concentrations of fluorochrome-conjugated antibodies at 4° C. in FACS buffer consisting of PBS with 2% FBS and 0.4% EDTA. All antibodies were anti-mouse and purchased from BD Bioscience or eBioscience and consisted of anti-CD4 (clones GK1.5 or RM4-5), anti-CD8 (clone 53-6.7), anti-CD278 (ICOS) (clone: 7E.17G9), anti-CD25 (clone PC61), anti-KLRG1 (clone 2F1), CD49b (Integrin alpha 2) (clone DX5), anti-CD3e (clone 1452C11), anti-CD45 (clone 30-F11), anti-CD69 PE (clone H1.2F3), anti-GITR (clone DTA-1), anti-Foxp3 (clone: FJK-16s) and Anti-Stat5 (clone 47/Stat5; pY694). Antibodies were conjugated to either FITC, PE, PerCP-CyTM5.5, PE-Cyanine7, APC, APC-eFluor® 780, eFluor® 450, or Alexa Fluor® 647.

Phospho-STAT5 evaluation was performed by paraformaldehyde fixation, methanol permeabilization and staining with AlexaFluor488-conjugated Anti-Stat5 (pY694) (BD Pharmingen; clone 612599). To accomplish this isolated NK cells or NK cells combined with NK-depleted splenocyte stromal cells were fixed in 2% paraformaldehyde (PFA) at 37° C. for 10 minutes after IL2 stimulation for 15 minutes. The cells were then washed once with ice-cold PBS and permeabilized by adding 0.5 ml/tube of 90% Methanol on ice for 1 hour. The cells were washed once with ice-cold PBS (to remove methanol), and stained for 1 hour with anti-Stat5 (pY694) antibody at room temperature followed by one wash in PBS/0.5% fetal calf serum.

In Vitro Cytotoxicity:

⁵¹Chromium release was conducted by incubating the target cells with 100 mCi sodium ⁵¹chromate (PerkinElmer) for 1 hour. Bulk splenocytes were used as effector cells and incubated with targets at defined effector:target ratios for 4 hours at 37° C. in round bottom 96 well plates. Specific lysis was expressed as (experimental release−spontaneous release)/(maximum release−spontaneous release)×100% with 0% specific lysis as lowest expressed value.

In Vivo Cytokine Injections:

For select experiment, the mice received intraperitoneal injections of cytokines in 200 μl volume given as ten equal doses given twice a day over a period of five days. As described above all cytokines were normalized to IUe on a molar basis. For select experiments, the mice were then sacrificed on day 6 and organs were fixed in 10% buffered formalin for histological analyses. For other experiments splenocyte and lung lymphocyte populations were analyzed flow cytometrically. For all the in vivo cytokine treatment experiments, animals were weighed (daily or every other day) and expressed as % change from start of cytokine therapy.

For evaluation of serum concentration wtIL2, mutIL2 or OMCP-mutIL2 were labeled with Alexa Fluor® 647 (LifeTechnologies Inc.) according to manufacturer instructions. Serum was collected at times specified and concentration of cytokine determined fluoroscopically according to a standard curve.

In Vivo Tumor Studies:

Lewis lung carcinoma (LLC) cells were subcutaneously injected into B6 or B6 NKG2D^−/− mice at 1×10⁵ cells per mouse in 100 μl of sterile saline. Once visible tumors were evident, day 5 post-injection, a five day course of cytokine treatment was started as described above. Measurement of cross sectional tumor diameter was performed using calipers and tumor volume estimated as 4/3πr³. The mice were sacrificed on day 24 post injection or once they reached a maximal tumor diameter of 20 mm. For NK cell depletion, mice were treated with anti-NK1.1 antibody (clone PK136) or mouse IgG isotype control (both from BioXcell) at 500 μg day −2, 250 μg day −1 and 250 μg weekly for the duration of the experiment. For lymphoma clearance experiments NJ mice were treated with ten doses of cytokine over a period of five days as described above and on day #6 injected intravenously with YAC-1 cells that were labeled with CFSE at 5×10⁶ cells/mouse. Mice were sacrificed 4 hours later, lungs were digested and viability of YAC-1 determined by forward and side scatter analysis of CFSE⁺ cells.

Statistics:

Comparison of splenic and lung-resident lymphocytes between various cytokine treatment conditions was performed by unpaired T-test with Welch's correction to account for unequal variance or unequal sample size. Tumor growth between different cytokine conditions was compared by multiple unpaired-T tests performed between various conditions at various time points using the Sidak-Bonferroni correction. Fold change in STAT5 phosphorylation was evaluated by unpaired T-test with Welch's correction in a similar fashion.

REFERENCES FOR EXAMPLES 1-6

• 1. Spangler, J. B. et al. Antibodies to Interleukin-2 Elicit Selective T Cell Subset Potentiation through Distinct Conformational Mechanisms. Immunity 42, 815-825 (2015).
• 2. French, A. R. et al. DAP12 signaling directly augments proproliferative cytokine stimulation of NK cells during viral infections. J Immunol 177, 49814990 (2006).
• 3. Rosenberg, S. A. et al. Experience with the use of high-dose interleukin-2 in the treatment of 652 cancer patients. Annals of surgery 210, 474-484; discussion 484-475 (1989).
• 4. Rosenberg, S. A. IL2: the first effective immunotherapy for human cancer. J

Immunol 192, 5451-5458 (2014).

• 5. Atkins, M. B. et al. High-dose recombinant interleukin 2 therapy for patients with metastatic melanoma: analysis of 270 patients treated between 1985 and 1993. J Clin Oncol 17, 2105-2116 (1999).
• 6. Sim, G. C. et al. IL2 therapy promotes suppressive ICOS⁺ Treg expansion in melanoma patients. J Clin Invest 124, 99-110 (2014).
• 7. Kolitz, J. E. et al. Recombinant interleukin-2 in patients aged younger than 60 years with acute myeloid leukemia in first complete remission: results from Cancer and Leukemia Group B 19808. Cancer 120, 1010-1017 (2014).
• 8. Krieg, C., Letourneau, S., Pantaleo, G. & Boyman, O. Improved IL2 immunotherapy by selective stimulation of IL2 receptors on lymphocytes and endothelial cells. Proc Natl Acad Sci USA 107, 11906-11911 (2010).
• 9. Heaton, K. M., Ju, G. & Grimm, E. A. Human interleukin 2 analogues that preferentially bind the intermediate-affinity interleukin 2 receptor lead to reduced secondary cytokine secretion: implications for the use of these interleukin 2 analogues in cancer immunotherapy. Cancer Res 53, 2597-2602 (1993).
• 10. Ullrich, E., Koch, J., Cerwenka, A. & Steinle, A. New prospects on the NKG2D/NKG2DL system for oncology. Oncoimmunology 2, e26097 (2013).
• 11. Raulet, D. H. Roles of the NKG2D immunoreceptor and its ligands. Nat Rev Immunol 3, 781-790 (2003).
• 12. Raulet, D. H., Gasser, S., Gowen, B. G., Deng, W. & Jung, H. Regulation of ligands for the NKG2D activating receptor. Annu Rev Immunol 31, 413-441 (2013).
• 13. Giuliani, E., Vassena, L., Cerboni, C. & Doria, M. Release of Soluble Ligands for the Activating NKG2D Receptor: One More Immune Evasion Strategy Evolved by HIV-1 ? Current drug targets (2015).
• 14. Campbell, J. A., Trossman, D. S., Yokoyama, W. M. & Carayannopoulos, L. N. Zoonotic orthopoxviruses encode a high-affinity antagonist of NKG2D. J Exp Med 204, 1311-1317 (2007).
• 15. Lazear, E., Peterson, L. W., Nelson, C. A. & Fremont, D. H. Crystal structure of the cowpox virus-encoded NKG2D ligand OMCP. J Virol 87, 840-850 (2013).
• 16. Kreisel, D. et al. Strain-specific variation in murine natural killer gene complex contributes to differences in immunosurveillance for urethane-induced lung cancer. Cancer Res 72, 4311-4317 (2012).
• 17. Frese-Schaper, M. et al. Influence of natural killer cells and perforinmediated cytolysis on the development of chemically induced lung cancer in NJ mice. Cancer Immunol Immunother 63, 571-580 (2014).
• 18. Dandamudi, U. B. et al. A phase II study of bevacizumab and high-dose interleukin-2 in patients with metastatic renal cell carcinoma: a Cytokine Working Group (CWG) study. J Immunother 36, 490-495 (2013).
• 19. Boyman, O., Kovar, M., Rubinstein, M. P., Surh, C. D. & Sprent, J. Selective stimulation of T cell subsets with antibody-cytokine immune complexes. Science 311, 1924-1927 (2006).
• 20. Smyth, M. J. et al. CD4+CD25+ T regulatory cells suppress NK cell-mediated immunotherapy of cancer. J Immunol 176, 1582-1587 (2006).
• 21. Chang, S. et al. Unique pulmonary antigen presentation may call for an alternative approach toward lung cancer immunotherapy. Oncoimmunology 2, e23563 (2013).
• 22. Plonquet, A. et al. Peripheral blood natural killer cell count is associated with clinical outcome in patients with aaIPI 2-3 diffuse large B-cell lymphoma. Annals of oncology: official journal of the European Society for Medical Oncology/ESMO 18, 1209-1215 (2007).
• 23. Tzeng, A., Kwan, B. H., Opel, C. F., Navaratna, T. & Wittrup, K. D. Antigen specificity can be irrelevant to immunocytokine efficacy and biodistribution. Proc Natl Acad Sci USA 112, 3320-3325 (2015).
• 24. Letourneau, S. et al. IL2/anti-IL2 antibody complexes show strong biological activity by avoiding interaction with IL2 receptor alpha subunit CD25. Proc Natl Acad Sci USA 107, 2171-2176 (2010).
• 25. Ho, E. L. et al. Costimulation of multiple NK cell activation receptors by NKG2D. J Immunol 169, 3667-3675 (2002).
• 26. Levin, A. M. et al. Exploiting a natural conformational switch to engineer an interleukin-2 ‘superkine’. Nature 484, 529-533 (2012).
• 27. Mitra, S. et al. Interleukin-2 activity can be fine tuned with engineered receptor signaling clamps. Immunity 42, 826-838 (2015).
• 28. Boyman, O. et al. Selectively expanding subsets of T cells in mice by injection of interleukin-2/antibody complexes: implications for transplantation tolerance. Transplantation proceedings 44, 1032-1034 (2012).
• 29. Tomala, J. et al. Chimera of IL2 linked to light chain of anti-IL2 mAb mimics IL2/anti-IL2 mAb complexes both structurally and functionally. ACS chemical biology 8, 871-876 (2013).
• 30. Gutbrodt, K. L., Casi, G. & Neri, D. Antibody-based delivery of IL2 and cytotoxics eradicates tumors in immunocompetent mice. Molecular cancer therapeutics 13, 1772-1776 (2014).
• 32. Yamane, B. H., Hank, J. A., Albertini, M. R. & Sondel, P. M. The development of antibody-IL2 based immunotherapy with hu14.18-IL2 (EMD-273063) in melanoma and neuroblastoma. Expert opinion on investigational drugs 18, 991-1000 (2009).
• 33. Carmenate, T. et al. Human IL2 mutein with higher antitumor efficacy than wild type IL2. J Immunol 190, 6230-6238 (2013).
• 34. Heaton, K. M. et al. Characterization of lymphokine-activated killing by human peripheral blood mononuclear cells stimulated with interleukin 2 (IL2) analogs specific for the intermediate affinity IL2 receptor. Cellular immunology 147, 167-179 (1993).
• 35. Imai, K., Matsuyama, S., Miyake, S., Suga, K. & Nakachi, K. Natural cytotoxic activity of peripheral-blood lymphocytes and cancer incidence: an 11-year follow-up study of a general population. Lancet 356, 1795-1799 (2000).
• 36. Lazear, E. et al. Cowpox virus OMCP antagonizes NKG2D via an unexpected binding orientation. PLos Pathogen In revision (2014).
• 37. Deng, W. et al. Antitumor immunity. A shed NKG2D ligand that promotes natural killer cell activation and tumor rejection. Science 348, 136-139 (2015).
• 38. Gorelik, E. & Herberman, R. B. Susceptibility of various strains of mice to urethan-induced lung tumors and depressed natural killer cell activity. J Natl Cancer Inst 67, 1317-1322 (1981).
• 39. Mancia, F. et al. Optimization of protein production in mammalian cells with a coexpressed fluorescent marker. Structure 12, 1355-1360 (2004).
• 40. Hank, J. A. et al. Distinct clinical and laboratory activity of two recombinant interleukin-2 preparations. Clin Cancer Res 5, 281-289 (1999).

Introduction to Examples 7-10

Intracellular surveillance mediated by MHC class I (MHCI) is a critical host immune function and as such MHCI molecules are frequently targeted for destruction or intracellular retention by viruses [1]. Many herpesviruses encode at least one protein that prevents the cell surface expression of MHCI [1,2]. However, this immune evasion strategy renders the infected cell susceptible to NK cell-mediated lysis due to loss of inhibitory signals [3]. Viral infection also leads to cell surface display of NKG2D ligands (NKG2DLs) recognized by the activating receptor NKG2D, further predisposing the infected cell towards NK cell-mediated lysis. Therefore, viruses that target MHCI expression often also sabotage NKG2D-mediated cell responses by targeting NKG2DLs on the infected cell [4-7].

NKG2DLs are not normally expressed on the cell surface but can be induced by cellular stress [8]. The specific trigger for NKG2DL expression is not known but NKG2DLs are upregulated in response to several viral infections [9-12]. NKG2DLs comprise a large group of proteins all recognized by NKG2D, despite having low sequence identity. NKG2DLs include the MIC (A and B) and ULBP (1-6) families in humans as well as MULTI and the RAE-1 (α-ε) and H60 (a-c) families in mice [13]. The redundancy in NKG2DLs is likely due to a combination of tissue specific expression patterns of the ligands and the need to counter viral NKG2D evasion strategies [14]. Many viruses have evolved mechanisms to inhibit the cell surface expression of NKG2DLs as a means of interfering with NKG2D surveillance of viral infection. This strategy is most apparent among β- and γ-herpesviruses, in which four murine cytomegalovirus proteins (m138, m145, m152, m155) [15-18], two human cytomegalovirus proteins (UL16, UL142) [19,20] and one Kaposi's sarcoma-associated herpesvirus protein (K5) [21] have been demonstrated to block NKG2DL surface expression. This evasion strategy is also found in RNA viruses, as hepatitis C virus NS3/4a and human immunodeficiency virus Nef proteins also block the expression of a subset of NKG2DLs [22,23]. Additionally, human cytomegalovirus, herpes simplex virus type 1 and Epstein-Barr virus each also encode at least one miRNA that prevents translation of MICB [24,25]. Similarly, JCV and BKV polyoma viruses target ULBP3 with miRNAs [26]. However, blocking NKG2DL expression on the infected cell is an imperfect evasion strategy, since no single viral protein or miRNA has been shown to block the expression of all NKG2DLs.

Like several herpesviruses, cowpoxvirus (CPXV) also sabotages MHCI expression. CPXV expresses CPXV012 and CPXV203, two proteins that prevent TAP-mediated peptide transport and MHCI trafficking to the cell surface, respectively [27-34]. Ectromelia virus, a related orthopoxvirus, induces NKG2DL expression and NKG2D is critical for the control of ectomelia virus pathogensis [35]. Infection with another orthopoxvirus, monkeypox virus, leads to dramatic expansion of NK cells but impaired NK cell function [36]. Together this suggests that CPXV infected cells would be sensitive to NK cell-mediated lysis.

Unlike herpesviruses, CPXV does not target NKG2DLs. Instead this virus targets NKG2D directly by encoding a competitive inhibitor of NKG2DLs, orthopoxvirus MHC class I-like protein (OMCP) [37,38]. OMCP is a 152 residue protein that is secreted from infected cells and antagonizes the NKG2D-mediated killing of NKG2DL-expressing target cells [37]. OMCP also plays an important role in vivo, with OMCP-null CPXV attenuated in mouse models of infection (M. Sun et al, personal communication). OMCP binds to murine NKG2D with an affinity equal or greater than all tested murine NKG2DLs, and to human NKG2D with an affinity ˜5,000-fold higher than human NKG2DLs [37-40].

Despite their divergence in sequence identity, all known host NKG2DLs share common structural features [41,42]. NKG2DLs contain an MHCI-like platform domain composed of an eight-stranded beta sheet with two helices [43-47]. The platform domain is subdivided into α1 and α2 domains, with each domain containing four beta strands and an alpha helix. Unlike MHCI, the groove between the helices of the NKG2DL platform domain is closed and therefore NKG2DLs do not bind peptides.

Like host NKG2DLs, OMCP also adopts an MHCI-like platform domain [38]. However, the platform domain of OMCP has been trimmed to have only a six-stranded beta sheet with shorter flanking helices. We termed the helix of the α1 domain H1 and the discontinuous helix of the α2 domain is termed H2a and H2b. The H2a and H2b helices of OMCP are also rearranged to be flatter against the beta sheet and to be splayed apart from each other. These differences in the OMCP structure were hypothesized to be important for the high affinity binding of OMCP to NKG2D. However, OMCP was still expected to bind to NKG2D in the same orientation as host NKG2DLs, i.e. with the alpha helices oriented diagonally within the symmetric NKG2D binding groove.

Here we report the 2.0 Å-resolution structure of human NKG2D bound to OMCP of the Brighton Red strain of cowpoxvirus. The structure reveals a significant reorientation of OMCP in the NKG2D binding groove relative to host NKG2DLs. The interface of OMCP with NKG2D is highly complementary, buries a significantly larger surface area than host NKG2DLs, and remains continuous across the entire NKG2D binding groove. This novel binding adaptation and high affinity allows OMCP to compete with the high local concentration of membrane-associated host NKG2DLs. We further show that the mechanism of NKG2D antagonism requires OMCP to be secreted, lest it lead to NKG2D signaling.

Example 7. Structure Determination of OMCP-NKG2D

We had previously solved the structure of OMCP alone and shown that, similar to host NKG2DLs, OMCP adopts an MHCI-like platform domain [38]. Despite the overall similarity of the domain structure of OMCP to host NKG2DLs, OMCP had several notable deviations in the putative NKG2D-binding site that were hypothesized to be important for the high affinity binding of OMCP to NKG2D. To further understand the unusually high affinity of OMCP for NKG2D, we crystallized and solved the structure of OMCP bound to human NKG2D.

Initial crystallization trials with OMCP and NKG2D yielded ˜30 different crystallization conditions. Subsequent data collection and molecular replacement of multiple low-resolution crystal forms all yielded similar partial solutions, with alternating sheets of OMCP-NKG2D complexes separated by undefined density. In the original structure of OMCP alone, the beta sheets packed to form a trimer with the alpha helices oriented away from the center [38]. An identical OMCP trimer formed in the OMCP-NKG2D partial solutions, with NKG2D now bound to the outward facing helices (data not shown). In an attempt to change the lattice packing, we introduced mutations into the beta sheet of OMCP that were designed to break the trimeric interface. These mutations were on the opposite face of OMCP from the NKG2D binding site to avoid disrupting OMCP-NKG2D binding. A mutant form of OMCP (Y23D, F95D) crystallized with NKG2D in a new space group and the crystals diffracted to 2.0 Å (Table 1)(FIG. 24A).

The electron density map was continuous and unambiguous throughout all chains of the structure, with the exception of Q108 in OMCP. This residue was situated in the center of the largest loop of OMCP and unambiguous density for this residue was also absent from the structure of OMCP alone [38]. The structure of OMCP bound to NKG2D showed no major differences from our previous structure of OMCP alone, with an RMSD for all atoms of 0.8 Å. Likewise, NKG2D was also similar to previous NKG2D structures with RMSDs ranging from 0.5-0.9 Å. The β3-β4 loop of NKG2D is the only region of either OMCP or NKG2D that displayed above-average B factors. This loop is thought to be flexible and has had above average B factors in all previous NKG2D structures [48]. Interestingly, the peptide bond between S193-S194 in our NKG2D structure had a cis conformation not described in other NKG2D structures (FIG. 29 ).

Example 8. The Interface Between OMCP and NKG2D

OMCP was hypothesized to bind to the same surface of NKG2D used by host NKG2DLs because (i) OMCP competed with host NKG2DLs for NKG2D and (ii) mutations within the NKG2DL-binding pocket of NKG2D altered OMCP binding affinity [38]. OMCP does bind NKG2D using the same concave binding pocket as host NKG2DLs (FIG. 24A). OMCP binds primarily using the discontinuous helices of its a2 domain, H2a and H2b. The position of the H2a and H2b helices is such that every surface exposed side chain of both helices within the binding site directly contacts NKG2D (FIG. 24B). Only two contacts are found outside of H2a and H2b, Ile49 and Arg66. Both of these residues are within the α1 domain but lie outside of the H1 helix.

Twelve OMCP residues contact eighteen NKG2D residues to form a mixture of bond types (Table 2). Three residues in each NKG2D half-site are known as core binding residues because they make contacts with all known host NKG2DLs. The core residues of NKG2D subunit A (NKG2D^A) (Tyr152, Tyr199, Met184) form two hydrogen bonds and make extensive hydrophobic contacts with OMCP residues. The core residues of NKG2D^A contact four OMCP residues and the most critical of these residues is Phe122. Phe122 makes multiple hydrophobic contacts with all three NKG2D^A core residues, including pi-stacking with Tyr152. Phe122 also forms a backbone-to-sidechain hydrogen bond with Tyr152. Interestingly, OMCP is the first NKG2D ligand not to utilize all six NKG2D core-binding residues, with only Met184 and Tyr152 of NKG2D subunit B (NKG2D^B) contacting OMCP. NKG2D^B Met184 and Tyr152 each make a single hydrogen bond and hydrophobic contacts with OMCP residues. Two OMCP residues, Trp127 and Asp132, make contacts with both NKG2D protomers. OMCP Trp127 forms a hydrogen bond to Lys150 of NKG2D^A and makes several hydrophobic contacts with Leu148 of NKG2D^B, Lys150 and Ser151 of NKG2D^A. OMCP Asp132 forms a hydrogen bond with Tyr152 of NKG2D^B and a salt bridge with Lys150 of NKG2D^A (FIG. 25A).

Due to the high affinity of the OMCP-NKG2D interaction we harnessed a high throughput in vitro selection approach to find NKG2D-binding null mutants (Table 3). The results of the screen identified D132 as an important residue for disrupting NKG2D binding. We then generated the mutation D132R in attempt to completely ablate NKG2D binding. Surprisingly, the D132R mutant alone was unable to bind to NKG2D at concentrations 35-fold above the K_D (FIG. 25B), but did not affect binding of OMCP to FcRL5-expressing cells (FIG. 25C). This mutation is likely to cause significant steric clashes, as well as disrupting both interactions made by Asp132 to NKG2D^A Lys150 and NKG2D^B Tyr152 (FIG. 25A).

Previously, the 14-fold higher affinity of OMCP for human vs murine NKG2D was mapped to three amino acid substitutions in the β5′-β5 loop of NKG2D, abbreviated L2 [38]. In addition to the substitutions themselves (I182V, M184I and Q185P), the position of the loop between NKG2D orthologs differs. L2 in human NKG2D is bent towards the center of the concave binding cavity compared to L2 of murine NKG2D. Superimposition of murine NKG2D onto the human NKG2D-OMCP structure reveals that the contacts between OMCP and Met184 (mNKG2D residue 1200) in NKG2D^B and between Met184 (1200) and Glu 85 (P201) in NKG2D^A would be altered due to the different position of the murine (β5′-β5 loop (FIG. 26A-B). This alteration would disrupt contacts with three residues in OMCP H2a, three residues in H2b and Arg66 within the α1 domain. Of the contact residues of L2, Met184 makes the most significant contacts in both NKG2Ds (Table 2)(FIG. 26C). Critically, of the 58 NKG2D sequences available in GenBank, 54 conserve the Met184 and Glu185 found in the high affinity human NKG2D (FIG. 26D).

Eighteen OMCP variants have been described between different CPXV and MPXV strains [51]. In this study we have crystallized OMCP from the Brighton Red strain of CPXV which has >60% sequence identity with the highly conserved sequence of the other 17 OMCP variants, collectively termed OMCP_mpx. Of the 12 OMCP contact residues observed, 9 are identical to OMCP_mpx. Of the remaining contacts, all three are conservative hydrophobic substitutions (I49L, T1181 and M1351) (FIG. 27 ). OMCP_mpx binds to NKG2D and the substitutions in the NKG2D contact residues are unlikely to grossly affect the affinity of OMCP_mpx for NKG2D [37].

Example 9. A Novel NKG2D-Binding Adaptation

Host NKG2DLs have low sequence identity but overall similar structures, with MHCI-like platform domains binding diagonally across the symmetric binding groove created by the NKG2D homodimer [13,41,52]. Host ligands contact one NKG2D half site with H1 and the S1-S2 loop, and contact the second NKG2D half site with H2b. Despite the similar MHCI-like fold, OMCP binds the NKG2D binding groove in a novel orientation, rotating ˜45° relative to host NKG2DLs (FIG. 27 ). Instead of using H1 and S1-S2 loop like host ligands, OMCP has replaced these contacts with H2a. This rotation leads to the helices of OMCP being perpendicular to the NKG2D binding groove, instead of lying diagonally across it.

Two unique rearrangements of H2a and H2b make the OMCP orientation possible. The α2 helices of OMCP and host NKG2DLs are discontinuous, with the two shorter helices hinged relative to each other. For host ligands, the angle between H2a and H2b is ˜90°, positioning H2a away from the NKG2D interface. In contrast, OMCP has increased the hinge angle between the helices by ˜20°, leading to a α2 helix that is flatter relative to the beta sheet of OMCP. The flattening of the α2 helix allows H2a and H2b to closely complement the concave binding groove of the NKG2D homodimer (FIG. 24B). The tight fit of the α2 helix for NKG2D is reflected in the high shape complementarity (0.77) and buried surface area (2,612 Ų). In contrast, host NKG2DLs have shape complementarity ranging from 0.63-0.72 and buried surface areas ranging from 1,700-2,180 Ų [43,44,46].

The second unique feature of the α2 helix is the separation of H2a and H2b relative to each other. This region also contains a translation that completely separates H2a and H2b into two distinct helices. This translation is critical for NKG2D binding because it allows each helix to be directly centered on the core binding sites of each NKG2D monomer (FIG. 27 ). This creates a symmetric binding site on OMCP that recognizes the symmetric binding groove created by the NKG2D dimer. The symmetry between OMCP and NKG2D binding is in stark contrast to the canonical binding of an asymmetric host ligand to the symmetric NKG2D binding groove [52]. However, one element of asymmetry remains in the OMCP-NKG2D interaction because each NKG2D half-site recognizes an OMCP helix in a different N- to C-terminal orientation, demonstrating again the flexibility of NKG2Ds rigid adaptation recognition [41,53].

The contact sites between NKG2D and host NKG2DLs are made up of two patches centered on the core binding sites of NKG2D and H1/S1-S2 loop and H2b of NKG2DLs [41]. As a result, the interface of NKG2D with NKG2DLs is discontinuous, particularly in the center of the NKG2D binding groove (FIG. 27 ). Due to the unique orientation of OMCP, H2a and H2b make continuous contacts along the entire NKG2D binding groove (FIG. 27 ). The sidechains of OMCP Lys126, Trp127, Glu131 and Asp132 make contacts with residues in the center of the NKG2D binding groove and bridge the core binding sites on each NKG2D monomer (FIG. 24B). In particular, OMCP Trp127 is directed towards the center of the NKG2D dimer and makes hydrophobic contacts with residues on both NKG2D monomers, effectively closing any gaps in the binding interface.

Example 10. Signaling of NKG2D Upon Ligand Engagement

CPXV and MPXV-infected cells secrete OMCP, which can act as an NKG2D-antagonist [37]. This immune evasion strategy is reminiscent of cancer induced-NKG2DL shedding. Some cancer cells proteolytically cleave NKG2DLs from the cell surface using matrix metalloproteinases (MMPs), simultaneously preventing NKG2D-bearing lymphocytes from targeting the cancer cell, as well as creating soluble NKG2DLs to inhibit NKG2D in trans. Cell-associated NKG2DLs trigger NKG2D effector functions (FIG. 28A), while cancer-induced, soluble NKG2DLs block NKG2D function (FIG. 28B). Like shed NKG2DLs, OMCP is soluble and blocks NKG2D function in trans [37] (FIG. 28C). Unlike host NKG2DLs, OMCP binds NKG2D with a novel orientation. We therefore asked whether OMCP could serve as a NKG2D agonist in the context of the cell membrane, analogously to host NKG2D ligands. Since OMCP is a secreted protein, an artificially cell-associated OMCP was constructed by using a heterologous transmembrane domain from Thy1.1 [37] (FIG. 28D). To measure NKG2D-mediated cell killing, we stably transduced Ba/F3 cells with retroviral vectors expressing either the OMCP-Thy1.1 construct or host NKG2DLs. OMCP-Thy1.1-expressing target cells were killed equivalently to host NKG2DL-transduced target cells, indicating that despite its altered binding orientation, cell-associated OMCP was able to activate NKG2D signaling (FIG. 28E). Thus, OMCP must be secreted lest it active NKG2D-effector functions itself, despite potential loss of efficacy due to diffusion.

Discussion for Examples 7-10

While many viruses have adopted a general mechanism of NKG2D-sabotage by trying to retain multiple host-encoded NKG2D ligands within the infected cell, CPXV and MPXV take the very different approach of targeting NKG2D directly. Since NKG2D is monomorphic, this mechanism has the significant advantage of requiring a single protein to prevent NKG2D recognition of the infected cell. The large number of sequence-divergent host NKG2DLs and their associated polymorphisms are thought to be driven by selection from pathogen-encoded NKG2DL antagonists [14]. Likewise, viral NKG2L antagonists are under selective pressure from the diverse host NKG2DLs in a continual cycle of adaptation. Due to the need to recognize multiple NKG2DLs, NKG2D has a limited mutational space to adapt. The limited ability of NKG2D to mutate is yet another advantage of OMCP directly targeting NKG2D, instead of NKG2DLs.

Similarly to OMCP, some cancer cells shed host NKG2DLs to create their own soluble NKG2D antagonists. However, this strategy has the additional benefit of removing host NKG2DL from the surface of cancer cells. In contrast, CPXV and MPXV lack a known mechanism of blocking host NKG2DL surface expression. Secreted OMCP must then be able to compete efficiently against the high local concentration of multiple host NKG2DLs on the infected cell, as well as against diffusion away from the infected cell. One possible way to increase OMCP's ability to compete with host ligands would be to increase the avidity of OMCP by having multiple NKG2D-binding domains. However, a multimeric OMCP could crosslink NKG2D and potentially trigger NKG2D-mediated killing. Therefore, secreted OMCP must be monomeric to prevent aberrant NKG2D signaling. Thus to compensate for these deficiencies, OMCP must have the highest affinity possible to effectively compete against cell-associated host NKG2DLs [37,38]. The half-life of ligand-receptor interactions correlate well with physiological competitiveness [55]. OMCP binds human and murine NKG2D with half-lives of 348 and 54 seconds, respectively, compared to half-lives of 1.5-18 seconds for most NKG2DLs [38,44,56]. Indeed, the increased half-life for NKG2D allows OMCP to effectively antagonize NKG2D-mediated immunity in a murine infection model (M. Sun et al, personal communication).

To understand the molecular basis for the long half-life of OMCP for NKG2D, we previously determined the structure of OMCP alone, and here, we report the structure of OMCP bound to NKG2D. The structure of OMCP alone was grossly similar to that of host NKG2D ligands, containing an atypical MHCI-like platform domain. Host NKG2D ligands bind with the helices of their platform domains oriented diagonally within the symmetric binding groove of NKG2D. Thus it was expected that OMCP was a viral mimic of host NKG2D ligands and would interact with NKG2D analogously.

The structure of OMCP-NKG2D instead revealed a novel orientation for an NKG2D ligand in the NKG2D binding groove. Alterations within the α2 domain helix allow OMCP to arrange its helices perpendicularly within the binding groove. This reorientation places the H2a and H2b helices directly in contact with the core binding sites of NKG2D and also forms the largest and most continuous binding interface with NKG2D. Because the forces (hydrogen bonds, van der Waals, hydrophobic interactions) that mediate protein-protein interactions are individually weak, a large, continuous interface with high shape complementary allows for a cumulatively strong interaction between proteins. This change in the binding orientation of OMCP reveals how the MHCI-like platform used by host ligands can be adapted by a pathogen to enhance NKG2D binding.

Since host NKG2DLs and OMCP have a similar MHCI-like platform, it is reasonable to wonder why no host ligand has evolved an analogous high-affinity interaction with NKG2D. One likely reason is that the host immune response must be carefully calibrated to balance the need for protection against the threat of autoimmunity. Since the expression of NKG2DLs on the cell surface signals for effector functions, even a small amount of high affinity host ligand on the cell surface could trigger an immune response, and the resulting tissue damage could be deleterious for the host. Indeed, NKG2D-expressing cells and/or aberrant expression of host NKG2DLs have been implicated in diabetes, celiac disease and rheumatoid arthritis [57-60]. Viruses are not constrained by autoimmune selective pressures. Therefore, CPXV and MPXV were free to evolve a viral NKG2DL with the highest possible affinity to maximize immune evasion potential.

Interestingly, OMCP triggers NKG2D signaling when attached to a target cell membrane, despite the novel orientation of OMCP relative to host NKG2DLs. The interaction of host NKG2DLs with the dimeric NKG2D bears broad structural similarity to the interaction between MHC molecules with their cognate T cell receptors (TCRs). In both cases, the NKG2DL/MHC lies diagonally across the surface created by the dimeric NKG2D/TCR. However, there are several examples of MHC-TCR complexes that, like OMCP-NKG2D, interact with unconventional orientations [61-65]. Several of these complexes involved autoimmune MHC-TCR complexes that were tilted or rotated outside of the normal range for MHC-TCR complexes [61,65]. While these receptors could induce TCR signaling at high MHC concentrations, they failed to assemble characteristic immunological synapses [66]. A striking example of unconventional binding was found when an in vitro peptide library-MHC-TCR (H2-L^d-42F3) screen produced a p3A1-H2-L^d-42F3 complex with an interface rotated ˜40° relative to other H2-L^d-42F3 complexes. This rotation places the TCR nearly parallel with the MHC peptide-binding groove and shifted the interface center almost entirely on one of the MHC α helices—an orientation strikingly similar to the interface of OMCP-NKG2D [65]. Interestingly, the p3A1-H2-L^d-42F3 complex failed to induce TCR signaling [65]. Thus, unlike OMCP/NKG2D, the orientation of MHC relative to TCR is an important factor for signaling.

OMCP-NKG2D and p3A1-H2-L^d-42F3 have opposite signaling outcomes, despite having very similar orientations. TCR signaling requires co-receptor binding to either the α2/β2 or α3 domains of MHCII or MHCI, respectively. The failure of p3A1-H2-L^d-42F3 to signal, and of other unconventional MHC-TCR complexes to form true immunological synapses, is potentially due to the inability of co-receptors to form correct quaternary structures for signaling [64,65,67]. Signaling by NKG2D is not known to require co-receptor stimulation and the majority of NKG2DLs lack the co-receptor binding α2/β2 or α3 domains of true MHC molecules. This difference in co-receptor dependency likely explains why OMCP (when attached via transmembrane) is still competent to stimulate NKG2D-signaling compared to MHC-TCR complexes with unconventional binding orientations. Further, it suggests that clustering of NKG2D on the cell surface is the major determinant of NKG2D-mediated activation.

Methods for Examples 7-10

Identification of NKG2D-Binding Null Mutant D132R.

A high throughput in vitro selection approach based on combinatorial cell surface display was utilized to identify NKG2D-binding null mutants. The sequence of OMCP was globally mutagenized using error-prone PCR, and the mutated amplicons were spliced to a signal-less Thy1.1 cDNA via overlap extension PCR. This library of mutated OMCPs fused to unmutated Thy1.1 was cloned into the pMXs-IRES-EGFP retroviral transfer vector (kind gift of Toshio Kitamura, University of Tokyo) to generate a molecular library for transduction into Ba/F3 cells. The transductants were then sorted for green fluorescence and anti-Thy1.1 expression to yield a cellular library whose members all had surface expression of OMCP, filtering out mutations giving frameshifts, premature stop codons, and folding-incompetent OMCP. This OMCP library was sorted for NKG2D binding using NKG2D-tetramers. Sorted cells were cloned by limiting dilution and analyzed. The retroviral cassettes of cells lacking or having reduced NKG2D-binding activity were amplified and sequenced. Utilizing this approach, we identified Asp132 as a critical residue for NKG2D binding.

Protein Expression and Purification.

OMCP_BR and human NKG2D expression constructs were previously described [38]. The (D132R) OMCP_BR protein was prepared identically to WT OMCP_BR. (23D/95D) OMCP-NKG2D complex was reconstituted by oxidative co-refolding from purified inclusion bodies, as described previously [38]. Refolded protein was slowly diluted 10-fold with water and captured on a 5 ml HiTrap Q HP column (GE Healthcare) using a Profinia instrument (Bio-Rad). The captured protein was washed with 50 mM Tris, pH 8.5, 20 mM NaCl and bulk eluted with 50 mM Tris, pH 8.5, 250 mM NaCl. The eluted protein was then concentrated and further purified by gel filtration chromatography on a Superdex S75 column (16/60; Amersham Biosciences). Fractions containing mono-dispersed OMCP-NKG2D complex (˜50 KDa) were pooled and buffer exchanged into 25 mM Ammonium acetate pH 7.4.

Crystallization, Data Collection and Processing.

Native protein crystals were grown by hanging drop vapor diffusion at 20° C. by streak seeding into a well solution containing 15% PEG 3350, 0.2M MgCl2, 0.1M Bis-Tris pH 6.75. Crystals were cryoprotected with well solution containing 15% glycerol before flash freezing directly in a liquid nitrogen bath. Diffraction data were collected at the Advanced Light Source synchrotron (beam line 4.2.2). Native (23D/95D) OMCP-hNKG2D crystal diffraction data were collected at 100 K and at a wavelength of 1.00004 Å. Additional diffraction data statistics are summarized in Table 1. Data processing with HKL2000 [68] showed the crystals belonged to the primitive monoclinic space group P2₁ (space group #4). The asymmetric unit of the crystal contained two copies of the (23D/95D) OMCP-hNKG2D complex.

Model Building and Refinement.

The structures of human NKG2D (1MPU) [48] and OMCP (4FFE) [38] were used as search models for molecular replacement through Phenix [69]. Reiterative refinement and manual rebuilding were performed using Phenix and Coot [70], respectively. Both 2Fo-Fc and Fo-Fc maps were used for manual building and to place solvent molecules. The final model yielded an R_work of 16.6% and R_free of 21.4%, with 4% of all reflections set aside for free R factor cross-validation. Progress in refinement was also measured using the MOLPROBITY webserver [71]. The final Ramachandran statistics for the model were 98% favored and 0% outliers. Additional refinement statistics are summarized in Table 1. Images of structures were produced using the program PyMol [72].

Structure Analysis.

Analysis of the contact residues, buried surface area and shape complementarity of the OMCP-NKG2D interface were carried out using the programs Ligplot+ [73], PISA [74] and SC [75]. Structural programs as compiled by the SBGrid consortium [76]. Analysis of NKG2D conservation was performed using the ConSurf server [77-80]. GenBank numbers for species used in Consurf analysis are: Humans (30749494), Borean orangutan (21902299), Chimpanzee (57113989), Gibbon (332232684), Macaque (355785888), Green Monkey (63/506,3485), Common marmoset (380848799), Mouse (148667521), Brown rat (149049263), Guinea Pig (348569092), Ground squirrel (532114387), Deer mouse (589967905), Naked mole rat (512868733), Prairie vole (532053033), European Shrew (505834608), Star-nosed mole (507978716), Chinese hamster (537136230), and Cat (410963826).

Atomic Coordinates.

The atomic coordinates (accession code 4PDC) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics (Rutgers University, New Brunswick, N.J.)

In Vitro NK Cell Killing Assays.

Splenocytes from C57BL/6 mice were preactivated with 200 U/ml IL2 for 24 hours and used as cytotoxic effectors against stably transduced Ba/F3 cell lines in standard killing assays. Target cells were carboxyfluorescein succinimidyl ester (CFSE) labeled and co-incubated with activated splenocytes at 37° C., 5% CO2 for 4 hours at effector:target ratios of 10:1, 20:1, and 40:1. Killing percentage was determined by incorporation of the dead cell exclusion dye 7-amino-actinomycin D (7AAD) in the CFSE+ target population as assessed by flow cytometry. Percent specific lysis was calculated using the formula [(experimental dead %−background dead %)/(maximum release dead %−background dead %)]×100. C57BL/6 mice were obtained from the National Cancer Institute (Charles River, Mass.). Mice were maintained under specific pathogen-free conditions and used between 8 and 12 weeks of age. Single cell suspensions of splenocytes used in killing assays were generated using standard protocols [81].

TABLE 1
Data collection and refinement statistics

	Data collection	OMCPBR-hNKG2D
	Space group	P21
	Cell dimensions
	a, b, c (Å)	43.3, 101.1, 91.4
	α, β, γ (°)	90.0, 91.6, 90.0
	Resolution (Å)	50-2.0 (2.07-2.00)
	Rsym	11.8 (48.5)
	I/σ	14.5 (3.8)
	Completeness (%)	93.5 (91.5)
	Redundancy	6.2 (5.3)
	Refinement
	Resolution (Å)	44-2.0
	Total reflections	309693
	Unique reflection	50139
	Rwork	16.6% (21.0%)
	Rfree	21.4% (29.5%)
	Wilson B-factor	21.62
	Protein residues	791
	Water molecules	524
	R.M.S. deviations	0.003
	Bond lengths (Å)
	Bond angles (°)	0.79
	a As defined by PHENIX [69]

TABLE 2
Interface contacts between NKG2D and OMCP

	NKG2D-A	OMCP	Bond type
	Lys150	Asp132	Salt bridge
	Lys150	Trp127	H bond
	Lys150	Trp127	ϕ (3)
	Ser151	Lys126	H bond
	Ser151	Trp127	ϕ (1)
	Tyr152	Phe122	H bond
	Tyr152	Phe122	ϕ (9)
	Tyr152	Lys126	ϕ (5)
	Met184	Thr118	H bond
	Met184	Thr119	ϕ (1)
	Met184	Phe122	ϕ (5)
	Gln185	Arg66	ϕ (1)
	Leu191	Phe122	ϕ (1)
	Tyr199	Phe122	ϕ (4)
	Glu201	Arg66	Salt bridge
	Thr205	Arg66	H bond
	NKG2D-B	OMCP	Bond type
	Leu148	Trp127	ϕ (1)
	Ser151	Glu131	H bond
	Tyr152	Asp132	H bond
	Tyr152	Glu131	ϕ (3)
	Tyr152	Met135	ϕ (5)
	Ile182	Ile49	ϕ (2)
	Glu183	Arg142	Salt bridge
	Met184	Met135	ϕ (1)
	Met184	Arg138	ϕ (2)
	Met184	Arg142	H bond
	Lys186	Arg142	ϕ (1)
	Leu191	Met135	ϕ (1)
	Glu201	Arg138	Salt bridge
	Hydrogen bonds (H bonds), salt bridges and carbon-to-carbon hydrophobic interactions (ϕ) are shown for each contact residue. The number of hydrophobic interactions between contact residues is designated in parenthesis.

TABLE 3
NKG2D binding mutations identified through global

Amino	Frequency		Solvent
Acid	of Mutation	Associated Mutations	Accessible
D132
	4	D132N	++
		D132N, T31S, V68A
		D132G, K126N, D76V
		D132G, K126N, D76V
K126	4	K126N	++
		K126N, S71G
		K126N, D132G, D76V
		K126N, D132G, D76V
K125	2	K125E, F65C	−
		K125E, F92V
S120	2	S120Y	−
		S120Y, E10A, N56K
D76	2	D76V, D132G, K126N	++
		D76V, D132G, K126N
W116	2	W116R	−
		W116R, K113Q
R123	2	R123G, D26G, F50L	−
		R123G, D21V, F128L
E75	1	E75D	−
S71	1	S71G, K126N	++
F92	1	F92V, K125E	+
F65	1	F65C, K125E	−
K113	1	K113Q, W116R	+
E10	1	E10A, N56K, S120Y	++
N56	1	E10A, N56K, S120Y	++
D21	1	D21V, R123G, F128L	++
F128	1	D21V, R123G, F128L	−
D26	1	D26G, F50L, R123G	++
F50	1	D26G, F50L, R123G	−
T31	1	T31S, V68A, D132N	++
V68	1	T31S, V68A, D132N	+
I30	1	I30L, L51F, L64P, M135T	−
L51	1	I30L, L51F, L64P, M135T	−
L64	1	I30L, L51F, L64P, M135T	++
M135	1	I30L, L51F, L64P, M135T	++
R67	1	R67S, L117P, T119N, F122L	+
L117	1	R67S, L117P, T119N, F122L	−
T119	1	R67S, L117P, T119N, F122L	++
F122	1	R67S, L117P, T119N, F122L	++
Mutations were sequenced from 17 clones expressing mutagenized OMCP-Thy1.1. Clones were selected for reduced binding to NKG2D tetramers. The selected clones showed variable deficits in NKG2D binding. Each clone had 1-4 mutations in the amino acid sequence of OMCP (5 clones with 1 mutation; 4 clones with 2 mutations; 6 clones with 3 mutations; 2 clones with 4 mutations). Silent mutations are not indicated. Mutations are listed in the order of frequency sequenced from the selected clones, and mutations that occurred together within individual clones are listed where applicable. Clones highlighted in grey have at least one mutation in a solvent inaccessible residue that may alter the overall stability of OMCP.

REFERENCES FOR EXAMPLES 7-10

• 1. Hansen T H, Bouvier M (2009) MHC class I antigen presentation: learning from viral evasion strategies. Nat Rev Immunol 9: 503-513.
• 2. Griffin B D, Verweij M C, Wiertz E J (2010) Herpesviruses and immunity: the art of evasion. Vet Microbiol 143: 89-100.
• 3. Karre K, Ljunggren H G, Piontek G, Kiessling R (1986) Selective rejection of H-2-deficient lymphoma variants suggests alternative immune defence strategy. Nature 319: 675-678.
• 4. Orange J S, Fassett M S, Koopman L A, Boyson J E, Strominger J L (2002) Viral evasion of natural killer cells. Nat Immunol 3: 1006-1012.
• 5. Lisnic V J, Krmpotic A, Jonjic S (2010) Modulation of natural killer cell activity by viruses. Curr Opin Microbiol 13: 530-539.
• 6. Finton K A, Strong R K (2012) Structural insights into activation of antiviral NK cell responses. Immunol Rev 250: 239-257.
• 7. Li Y, Mariuzza R A (2014) Structural Basis for Recognition of Cellular and Viral Ligands by NK Cell Receptors. Front Immunol 5: 123.
• 8. Raulet D H (2003) Roles of the NKG2D immunoreceptor and its ligands. Nat Rev Immunol 3: 781-790.
• 9. Draghi M, Pashine A, Sanjanwala B, Gendzekhadze K, Cantoni C, et al. (2007) NKp46 and NKG2D recognition of infected dendritic cells is necessary for NK cell activation in the human response to influenza infection. J Immunol 178: 2688-2698.
• 10. Pappworth I Y, Wang E C, Rowe M (2007) The switch from latent to productive infection in epstein-barr virus-infected B cells is associated with sensitization to NK cell killing. J Virol 81: 474-482.
• 11. Welte S A, Sinzger C, Lutz S Z, Singh-Jasuja H, Sampaio K L, et al. (2003) Selective intracellular retention of virally induced NKG2D ligands by the human cytomegalovirus UL16 glycoprotein. Eur J Immunol 33: 194-203.
• 12. Ward J, Bonaparte M, Sacks J, Guterman J, Fogli M, et al. (2007) HIV modulates the expression of ligands important in triggering natural killer cell cytotoxic responses on infected primary T-cell blasts. Blood 110: 1207-1214.
• 13. Obeidy P, Sharland A F (2009) NKG2D and its ligands. Int J Biochem Cell Biol 41: 2364-2367.
• 14. Eagle R A, Trowsdale J (2007) Promiscuity and the single receptor: NKG2D. Nat Rev Immunol 7: 737-744.
• 15. Lodoen M, Ogasawara K, Hamerman J A, Arase H, Houchins J P, et al. (2003) NKG2D-mediated natural killer cell protection against cytomegalovirus is impaired by viral gp40 modulation of retinoic acid early inducible 1 gene molecules. J Exp Med 197: 1245-1253.
• 16. Lodoen M B, Abenes G, Umamoto S, Houchins J P, Liu F, et al. (2004) The cytomegalovirus m155 gene product subverts natural killer cell antiviral protection by disruption of H60-NKG2D interactions. J Exp Med 200: 1075-1081.
• 17. Krmpotic A, Hasan M, Loewendorf A, Saulig T, Halenius A, et al. (2005) NK cell activation through the NKG2D ligand MULT-1 is selectively prevented by the glycoprotein encoded by mouse cytomegalovirus gene m145. J Exp Med 201: 211-220.
• 18. Lenac T, Budt M, Arapovic J, Hasan M, Zimmermann A, et al. (2006) The herpesviral Fc receptor fcr-1 down-regulates the NKG2D ligands MULT-1 and H60. J Exp Med 203: 1843-1850.
• 19. Cosman D, Mullberg J, Sutherland C L, Chin W, Armitage R, et al. (2001) ULBPs, novel MHC class I-related molecules, bind to CMV glycoprotein UL16 and stimulate NK cytotoxicity through the NKG2D receptor. Immunity 14: 123-133.
• 20. Chalupny N J, Rein-Weston A, Dosch S, Cosman D (2006) Down-regulation of the NKG2D ligand MICA by the human cytomegalovirus glycoprotein UL142. Biochem Biophys Res Commun 346: 175-181.
• 21. Thomas M, Boname J M, Field S, Nejentsev S, Salio M, et al. (2008) Down-regulation of NKG2D and NKp80 ligands by Kaposi's sarcoma-associated herpesvirus K5 protects against NK cell cytotoxicity. Proc Natl Acad Sci USA 105: 1656-1661.
• 22. Cerboni C, Neri F, Casartelli N, Zingoni A, Cosman D, et al. (2007) Human immunodeficiency virus 1 Nef protein downmodulates the ligands of the activating receptor NKG2D and inhibits natural killer cell-mediated cytotoxicity. J Gen Virol 88: 242-250.
• 23. Wen C, He X, Ma H, Hou N, Wei C, et al. (2008) Hepatitis C virus infection downregulates the ligands of the activating receptor NKG2D. Cell Mol Immunol 5: 475-478.
• 24. Stern-Ginossar N, Elefant N, Zimmermann A, Wolf D G, Saleh N, et al. (2007) Host immune system gene targeting by a viral miRNA. Science 317: 376-381.
• 25. Nachmani D, Stern-Ginossar N, Sarid R, Mandelboim O (2009) Diverse herpesvirus microRNAs target the stress-induced immune ligand MICB to escape recognition by natural killer cells. Cell Host Microbe 5: 376-385.
• 26. Bauman Y, Nachmani D, Vitenshtein A, Tsukerman P, Drayman N, et al. (2011) An identical miRNA of the human JC and BK polyoma viruses targets the stress-induced ligand ULBP3 to escape immune elimination. Cell Host Microbe 9: 93-102.
• 27. Gainey M D, Rivenbark J G, Cho H, Yang L, Yokoyama W M (2012) Viral MHC class I inhibition evades CD8+ T-cell effector responses in vivo but not CD8⁺ T-cell priming. Proc Natl Acad Sci USA 109: E3260-3267.
• 28. Byun M, Verweij M C, Pickup D J, Wiertz E J, Hansen T H, et al. (2009) Two mechanistically distinct immune evasion proteins of cowpox virus combine to avoid antiviral CD8 T cells. Cell Host Microbe 6: 422-432.
• 29. Byun M, Wang X, Pak M, Hansen T H, Yokoyama W M (2007) Cowpox virus exploits the endoplasmic reticulum retention pathway to inhibit MHC class I transport to the cell surface. Cell Host Microbe 2: 306-315.
• 30. McCoy WHt, Wang X, Yokoyama W M, Hansen T H, Fremont D H (2013) Cowpox virus employs a two-pronged strategy to outflank MHCI antigen presentation. Mol Immunol.
• 31. McCoy WHt, Wang X, Yokoyama W M, Hansen T H, Fremont D H (2012) Structural mechanism of ER retrieval of MHC class I by cowpox. PLoS Biol 10: e1001432.
• 32. Alzhanova D, Edwards D M, Hammarlund E, Scholz I G, Horst D, et al. (2009) Cowpox virus inhibits the transporter associated with antigen processing to evade T cell recognition. Cell Host Microbe 6: 433-445.
• 33. Dasgupta A, Hammarlund E, Slifka M K, Fruh K (2007) Cowpox virus evades CTL recognition and inhibits the intracellular transport of MHC class I molecules. J Immunol 178: 1654-1661.
• 34. Luteijn R D, Hoelen H, Kruse E, van Leeuwen W F, Grootens J, et al. (2014) Cowpox Virus Protein CPXV012 Eludes CTLs by Blocking ATP Binding to TAP. J Immunol 193: 1578-1589.
• 35. Fang M, Lanier L L, Sigal L J (2008) A role for NKG2D in NK cell-mediated resistance to poxvirus disease. PLoS Pathog 4: e30.
• 36. Song H, Josleyn N, Janosko K, Skinner J, Reeves R K, et al. (2013) Monkeypox virus infection of rhesus macaques induces massive expansion of natural killer cells but suppresses natural killer cell functions. PLoS One 8: e77804.
• 37. Campbell J A, Trossman D S, Yokoyama W M, Carayannopoulos L N (2007) Zoonotic orthopoxviruses encode a high-affinity antagonist of NKG2D. J Exp Med 204: 1311-1317.
• 38. Lazear E, Peterson L W, Nelson C A, Fremont D H (2013) Crystal structure of the cowpox virus-encoded NKG2D ligand OMCP. J Virol 87: 840-850.
• 39. Carayannopoulos L N, Naidenko O V, Kinder J, Ho E L, Fremont D H, et al. (2002) Ligands for murine NKG2D display heterogeneous binding behavior. Eur J Immunol 32: 597-605.
• 40. Mistry A R, O'Callaghan C A (2007) Regulation of ligands for the activating receptor NKG2D. Immunology 121: 439-447.
• 41. Strong R K, McFarland B J (2004) NKG2D and Related Immunoreceptors. Adv Protein Chem 68: 281-312.
• 42. Deng L, Mariuzza R A (2006) Structural basis for recognition of MHC and MHC-like ligands by natural killer cell receptors. Semin Immunol 18: 159-166.
• 43. Li P, McDermott G, Strong R K (2002) Crystal structures of RAE-1beta and its complex with the activating immunoreceptor NKG2D. Immunity 16: 77-86.
• 44. Li P, Morris D L, Willcox B E, Steinle A, Spies T, et al. (2001) Complex structure of the activating immunoreceptor NKG2D and its MHC class I-like ligand MICA. Nat Immunol 2: 443-451.
• 45. Li P, Willie S T, Bauer S, Morris D L, Spies T, et al. (1999) Crystal structure of the MHC class I homolog MIC-A, a gammadelta T cell ligand. Immunity 10: 577-584.
• 46. Radaev S, Rostro B, Brooks A G, Colonna M, Sun P D (2001) Conformational plasticity revealed by the cocrystal structure of NKG2D and its class I MHC-like ligand ULBP3. Immunity 15: 1039-1049.
• 47. Adams E J, Luoma A M (2013) The adaptable major histocompatibility complex (MHC) fold: structure and function of nonclassical and MHC class I-like molecules. Annu Rev Immunol 31: 529-561.
• 48. McFarland B J, Kortemme T, Yu S F, Baker D, Strong R K (2003) Symmetry recognizing asymmetry: analysis of the interactions between the C-type lectin-like immunoreceptor NKG2D and MHC class I-like ligands. Structure 11: 411-422.
• 49. Stewart D E, Sarkar A, Wampler J E (1990) Occurrence and role of cis peptide bonds in protein structures. J Mol Biol 214: 253-260.
• 50. Craveur P, Joseph A P, Poulain P, de Brevern A G, Rebehmed J (2013) Cis-trans isomerization of omega dihedrals in proteins. Amino Acids 45: 279-289.
• 51. Lefkowitz E J, Upton C, Changayil S S, Buck C, Traktman P, et al. (2005) Poxvirus Bioinformatics Resource Center: a comprehensive Poxviridae informational and analytical resource. Nucleic Acids Res 33: D311-316.
• 52. Strong R K (2002) Asymmetric ligand recognition by the activating natural killer cell receptor NKG2D, a symmetric homodimer. Mol Immunol 38: 1029-1037.
• 53. Radaev S, Sun P D (2003) Structure and function of natural killer cell surface receptors. Annu Rev Biophys Biomol Struct 32: 93-114.
• 54. Campbell J A, Davis R S, Lilly L M, Fremont D H, French A R, et al. (2010) Cutting edge: FcR-like 5 on innate B cells is targeted by a poxvirus MHC class I-like immunoevasin. J Immunol 185: 28-32.
• 55. Copeland R A, Pompliano D L, Meek T D (2006) Drug-target residence time and its implications for lead optimization. Nat Rev Drug Discov 5: 730-739.
• 56. O'Callaghan C A, Cerwenka A, Willcox B E, Lanier L L, Bjorkman P J (2001) Molecular competition for NKG2D: H60 and RAE1 compete unequally for NKG2D with dominance of H60. Immunity 15: 201-211.
• 57. Groh V, Bruhl A, EI-Gabalawy H, Nelson J L, Spies T (2003) Stimulation of T cell autoreactivity by anomalous expression of NKG2D and its MIC ligands in rheumatoid arthritis. Proc Natl Acad Sci USA 100: 9452-9457.
• 58. Hue S, Mention J J, Monteiro R C, Zhang S, Cellier C, et al. (2004) A direct role for NKG2D/MICA interaction in villous atrophy during celiac disease. Immunity 21: 367-377.
• 59. Meresse B, Chen Z, Ciszewski C, Tretiakova M, Bhagat G, et al. (2004) Coordinated induction by IL15 of a TCR-independent NKG2D signaling pathway converts CTL into lymphokine-activated killer cells in celiac disease. Immunity 21: 357-366.
• 60. Ogasawara K, Hamerman J A, Hsin H, Chikuma S, Bour-Jordan H, et al. (2003) Impairment of NK cell function by NKG2D modulation in NOD mice. Immunity 18: 41-51.
• 61. Hahn M, Nicholson M J, Pyrdol J, Wucherpfennig K W (2005) Unconventional topology of self peptide-major histocompatibility complex binding by a human autoimmune T cell receptor. Nat Immunol 6: 490-496.
• 62. Sethi D K, Schubert D^A, Anders A K, Heroux A, Bonsor D^A, et al. (2011) A highly tilted binding mode by a self-reactive T cell receptor results in altered engagement of peptide and MHC. J Exp Med 208: 91-102.
• 63. Wucherpfennig K W, Call M J, Deng L, Mariuzza R (2009) Structural alterations in peptide-MHC recognition by self-reactive T cell receptors. Curr Opin Immunol 21: 590-595.
• 64. Yin Y, Li Y, Mariuzza R A (2012) Structural basis for self-recognition by autoimmune T-cell receptors. Immunol Rev 250: 32-48.
• 65. Adams J J, Narayanan S, Liu B, Birnbaum M E, Kruse A C, et al. (2011) T cell receptor signaling is limited by docking geometry to peptide-major histocompatibility complex. Immunity 35: 681-693.
• 66. Schubert D^A, Gordo S, Sabatino J J, Jr., Vardhana S, Gagnon E, et al. (2012) Self-reactive human CD4 T cell clones form unusual immunological synapses. J Exp Med 209: 335-352.
• 67. Li Y, Yin Y, Mariuzza R A (2013) Structural and biophysical insights into the role of CD4 and CD8 in T cell activation. Front Immunol 4: 206.
• 68. Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Macromolecular Crystallography, Pt A 276: 307-326.
• 69. Adams P D, Grosse-Kunstleve R W, Hung L W, loerger T R, McCoy A J, et al. (2002) PHENIX: building new software for automated crystallographic structure determination. Acta Crystallogr D Biol Crystallogr 58: 1948-1954.
• 70. Emsley P, Cowtan K (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60: 2126-2132.
• 71. Chen V B, Arendall W B, 3rd, Headd J J, Keedy D A, Immormino R M, et al. (2010) MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr D Biol Crystallogr 66: 12-21.
• 72. Schrodinger, LLC (2010) The PyMOL Molecular Graphics System, Version 1.3r1.
• 73. Laskowski R A, Swindells M B (2011) LigPlot+: multiple ligand-protein interaction diagrams for drug discovery. J Chem Inf Model 51: 2778-2786.
• 74. Krissinel E, Henrick K (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372: 774-797.
• 75. Lawrence M C, Colman P M (1993) Shape complementarity at protein/protein interfaces. J Mol Biol 234: 946-950.
• 76. Morin A, Eisenbraun B, Key J, Sanschagrin P C, Timony M A, et al. (2013) Collaboration gets the most out of software. Elife 2: e01456.
• 77. Ashkenazy H, Erez E, Martz E, Pupko T, Ben-Tal N (2010) ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids. Nucleic Acids Res 38: W529-533.
• 78. Landau M, Mayrose I, Rosenberg Y, Glaser F, Martz E, et al. (2005) ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures. Nucleic Acids Res 33: W299-302.
• 79. Glaser F, Pupko T, Paz I, Bell R E, Bechor-Shental D, et al. (2003) ConSurf: identification of functional regions in proteins by surface-mapping of phylogenetic information. Bioinformatics 19: 163-164.
• 80. Celniker G, Nimrod G, Ashkenazy H, Glaser F, Martz E, et al. (2013) ConSurf: Using Evolutionary Data to Raise Testable Hypotheses about Protein Function. Israel Journal of Chemistry 53: 199-206.
• 81. Dokun A O, Kim S, Smith H R, Kang H S, Chu D T, et al. (2001) Specific and nonspecific NK cell activation during virus infection. Nat Immunol 2: 951-956.

Example 11. Individuals with Poorly Functioning Natural Killer Cells are More Susceptible to Malignancies

FIG. 14A shows that AJ and 129 are lung cancer susceptible strain of mice and B6 and C3H are lung cancer resistant strains of mice based on the larger tumor burden found in AJ and 129 mice. FIG. 14B shows that when NK cells from the various mouse strains were incubated with LM2 lung carcinoma cells at varying ratios, the NK cells freshly isolated from B6 and C3H mice (lung cancer resistant strains) resulted in significantly more lysis of LM2 lung carcinoma cells than the NK cells freshly isolated from AJ and 129 mice (lung cancer susceptible strains). Taken together these data show that strains of mice that are resistant to lung cancer have NK cells that more effectively lyse lung carcinoma cells. Further, susceptible strains have poorly functioning NK cells.

That data also correlates with human data. FIG. 15 shows that a greater percentage of NK cells appear to produce TNFα in “resistant” patients versus “susceptible” patients. Further, it has been shown that tumors downregulate the lytic capacity of NK cells, even if they were highly functional before.⁵³ Thus, even individuals with highly functioning NK cells may benefit from therapy to enhance NK cell function.

Notably, ex vivo cytokine activation can reverse natural killer cell dysfuction. FIG. 16 shows that IL2 activated NK cells from both resistant (B6 and C3H) and susceptible (AJ and 129) mouse strains can lyse LM2 lung cancer cells. Accordingly, mouse NK Cells that did not show significant lysis of cancer cells (NK cells from 129 & AJ strains) were much more effective at lysis when treated with IL2. NK cells from cancer-resistant strains also showed increase % of specific lysis.

Example 12. OMCP-mutIL2 Mediated Immunotherapy In Vivo

Immunoregulation of malignancies involves an intricate interplay of multiple cellular components. CD4⁺Foxp3⁺ T_regs have been shown in multiple models to contribute to tumor-specific tolerance and facilitate tumor growth^{4, 16, 17}. NK cells and CD8⁺ CTLs contribute to immunoregulation of multiple tumors, such as melanoma^{12, 18}. Other tumors, such as lung cancer, are controlled almost exclusively by NK cells with little contribution by the adaptive immune system^{19, 20} (and unpublished data AS. Krupnick). In order to test OMCP-mutIL2 mediated immunotherapy we will rely on B16 melanoma expressing the model tumor antigen ovalbumin (MO5 tumor cell line)²¹. Multiple studies have demonstrated a role for both NK cells and CD8⁺ CTLs in controlling melanoma growth^22-24. Thus the melanoma model offers an experimental advantage in studying OMCP-mutIL2, which can activate both types of cells (FIG. 1E-F). Reagents specific to this tumor, such as tetramers for the MHC Class I-restricted CD8⁺ T cell receptor specific for the melanoma tumor associated antigen tyrosinase-related protein 2 peptide SVYDFFVWL (SEQ ID NO:3), can be readily purchased commercially (Proimmune, Sarasota, Fl.). The use of an ovalbum in-expressing cell line also offers the advantage of studying the immune response to a the highly immunogenic peptide SIINFEKL (SEQ ID NO:4) in addition to naturally occurring tumor associated antigens such as tyrosinase-related protein 2 which generally expands T cells with low avidity^{25, 26}.

In order to perform the studies B6 mice will be injected subcutaneously with 1×10⁶ MO5 melanoma cells. One week after tumor injection mice will be divided into 4 groups (10 mice per group) and treated with ten twice a day injections of either: wild type IL2 (group #1); mutIL2 (group #2); OMCP-mutIL2 (group #3) or; saline (group #4) (FIG. 12 ). Tumor growth will be followed by daily measurements of diameter for 4 weeks, or until one of the groups develops tumors >2 cm in diameter. At that point mice in all groups will be sacrificed for analysis. In addition to tumor growth, lymphocyte infiltration of both the tumor and draining inguinal lymph node will be evaluated by flow cytometry. We will quantitate the total number and activation status of CD4⁺Foxp3+ T_regs (evaluated by ICOS and GITR upregulation). We will also evaluate NK cell number and activation as measured by IFN-γ production and CD69 upregulation. Antigen-specific CTL generation will be evaluated by quantitating both CD8⁺ T cells and CD8⁺CD44^hiCD62^low effector cells (ECs) that are primarily responsible for tumor clearance^{22, 27, 28}. Antigen specificity will be determined by identifying CD8⁺ CTLs with T cell receptor specific for either the ovalbumin peptide SIINFEKL (SEQ ID NO:4) or melanoma specific tyrosinase-related protein 2 peptide SVYDFFVWL (SEQ ID NO:3) (both tetramers from Proimmune, Sarasota, Fl.). Tumor apoptosis will be quantitated by TUNEL staining.

Based on our in vitro tumor data and in vivo phenotypic analysis we suspect that the OMCP-mutIL2 group will demonstrate attenuation in tumor growth with high number of NK cells, antigen-specific CTLs, specifically CD8⁺ ECs, and fewer CD4⁺Foxp3⁺ T_regs. If this turns out to be the case we would determine the relative role for CD8⁺ or NK CTLs by depletion experiments. Even if CTLs increase it is possible that M05 growth will not be altered. If that turns out to be the case we would look in closer detail at the CD4⁺Foxp3⁺ T_regs or in the presence and activation of myeloid-derived suppressor cells in OMCP-mutIL2 treated mice. Based on melanoma data additional tumors will be tested using similar methods.

Example 13. CD8⁺ Memory T Cell Generation after Treatment with OMCP-mutIL2 Fusion Construct

Once activation through their T cell receptor, naive CD8⁺ T cells primarily differentiate into short-lived CD44^hiCD62^low effector cells (ECs) with cytolytic potential. A portion of activated cells, however, differentiate to long-lived CD44^hiCD62L^hi central memory T cells (CD8⁺ CMs)^29-31. CD8⁺ CMs act as an antigen specific reservoir for cellular protection and upon restimulation differentiate into CD8⁺ ECs with cytolytic function. The durability of CD8⁺ CMs makes them an ideal target for ex vivo generation and adoptive transfer for long-term protection³¹. The possibility of generating this cell population in vivo offers multiple advantages over an ex vivo system, including establishing a polyclonal population reactive to multiple tumor associated antigens and avoidance of costs associated with donor pheresis and ex vivo expansion. In vivo expansion of tumor antigen specific CD8⁺ CMs could also eliminate the need for frequent pheresis and cell readministration.

High dose IL2 therapy results in activation of both CD4⁺Foxp3⁺ T_regs and CD8⁺ T cells but its effect on tumor associated antigen specific CD8⁺ CM generation is unknown. Some have demonstrated, using antibody depletion, that CD4⁺Foxp3⁺ T_regs interfere with tumor specific CD8⁺ CM generation^{17, 32} while others, using different models, have demonstrated that CD4⁺Foxp3⁺ T_reg depletion impairs CD8⁺ memory formation^{33, 34}. OMCP-mutIL2 creates a unique immunologic environment where CD4⁺Foxp3⁺ T_regs are maintained but not actively expanded (FIG. 3 ). While NKG2D is not expressed on resting CD8⁺ T cells, it is induced on this population upon activation³⁵. Thus, unlike mutIL2, OMCP-mutIL2 results in CD8⁺ T cell proliferation at levels comparable to wild-type IL2 in NKG2D-sufficient mice (FIG. 1E-F). The effect of OMCP-mutIl2 on CD8⁺ T cell memory formation, however, is unknown but is critical to decipher based on the long-term tumor specific immunity that this cell population can confer.

In order to test long-term memory formation after cytokine stimulation in vivo we will utilize a model of irradiated tumor cell vaccination and cytokine treatment. In order to accomplish this we will subcutaneously inject 1×10⁷ lethally irradiated (10 Gy) M05 melanoma cells into C57131/6 mice. The recipient mice will then be treated either regular IL2 (group #1), mutIL2 (group #2), OMCP-mutIL2 (group #3) or saline (group #4) in twice daily doses over a course of 5 days (FIG. 13 ). The mice will be sacrificed at various time points ranging from one to three months post infection (FIG. 13 ). Antigen-specific CD8⁺ CM formation will be assessed by phenotypic analysis of splenic, peripheral lymph node, lung, and liver-resident CD8⁺ CD44^hiCD62L^hi CMs. Antigen specificity will be determined by MHC Class I staining for either the ovalbumin peptide, SIINFEKL (SEQ ID NO:4), or melanoma specific tyrosinase-related protein 2 peptide SVYDFFVWL (SEQ ID NO:3) (both from Proimmune, Sarasota, Fl.).

In order to test the functional protection of such vaccination protocols in a separate set of experiments mice from the four groups described above will not be sacrificed for phenotypic analysis and will be reinjected with live M05 melanoma (1×10⁶ cells/mouse subcutaneously). Melanoma growth will be assessed by serial measurement of tumor diameter. Contribution of CD8⁺ T cells to any immunologic protection will be assessed by CD8-specific antibody depletion in a portion of mice (clone YTS 169.4, BioXcell Inc., West Lebanon, NH).

Example 14. Mechanism of CTL Activation by OMCP-mutIL2 Fusion Construct

A mechanistic understanding of the enhanced activation of effector cell function by the OMCP-mutIL2 chimera will be critical for optimizing this therapeutic agent. The interaction of the fusion protein with IL2R and NKG2D are likely to be dependent on several factors including the length of the linker peptide (FIG. 1E-F). Therefore, it is critical to understand the mechanism of OMCP-mutIL2 chimera mediated CTL activation in order to allow for optimization of the construct and design of future immunotherapy protocols. The two-domain chimeric protein could potentially increase the activation of NKG2D-expressing cells by three non-mutually exclusive mechanisms. First and foremost the OMCP-mutIL2 construct could increase the avidity of mutIL2 binding to targeted cells. This could lead to an increase in the number of receptors occupied and increased signaling intensity compared to mutIL2. Additionally dual binding to both NKG2D and IL2R could decrease the rate of receptor internalization and increase the duration of signaling by IL2. It is also possible that the OMCP-mutIL2 construct alters the signaling profile by the target cell by activating both the IL2 and NKG2D stimulatory pathways. These three non-mutually exclusive effects could explain the increase in activation of our construct of CTLs in an NKG2D-mediated fashion.

There are several methods for determining the avidity of a protein for a cell, either directly (radiolabeled, fluorescent) or indirectly (antigen exclusion)^{38, 39}. We plan to determine the avidity of wild-type IL2, mutIL2, or OMCP-mutIL2 for CD4⁺Foxp3+ T_regs, NK cells, and CD8⁺ T lymphocytes using KinExA⁴⁰. To accomplish this we will isolate cells from splenocytes of either wild-type C57Bl/6 or NKG2D^−/− mice on a C57Bl/6 background using a magnetic bead isolation kit (Miltenyi Biotech, San Diego, Calif.). Target cells will be serially diluted by a factor of 2 in 11 falcon tubes in media containing 0.05% NaN₃. The 12th tube will contain just the media. OMCP-mutIL2 or mutIL2 alone will then be added to each tube of either wild-type or NKG2D^−/− cells and the cells with cytokine will be rotated at 4° C. for 36 h. At the end of 36 h, the cells were centrifuged at 2400 rpm for 4 min and the free construct present in the supernatant will be measured by an anti-IL2 ELISA. The equilibrium dissociation constant (Kd) will then be calculated⁴¹. This approach has the advantage of measuring the avidity of cell surface molecules at physiologic densities and obviates the need for labeling, which can artificially lower the affinity of antibodies for their antigens^{42, 43}.

The two-domain structure of the fusion protein is likely to significantly increase the half-life of the protein on the surface of NKG2D⁺ and IL2R⁺ cells. Any increase in surface half-life likely affects both the internalization of the bound receptors and signaling intensity and duration. To address the internalization of receptors, we will incubate each construct with the above mentioned cell types over a range of times and monitor the change in cell surface expression of IL2Rβγ and NKG2D using flow cytometry as previously described⁴⁴. Of key interest will be the signaling profile of each construct. IL2-IL2R engagement signals through JAK-STAT pathways, while NKG2D signals through DAP10/12 pathways. While monomeric, soluble OMCP does not induce NKG2D signaling, OMCP can signal when concentrated locally on the cell surface⁴⁵. Therefore, it is critical to determine whether the chimera is capable of inducing dual signaling through IL2R and NKG2D. IL2-mediated signaling will be assessed by Western blot for phosphorylated JAK1 and JAK3 in freshly isolated CD4⁺Foxp3⁺ T_regs, NK cells or CD8⁺ T cells incubated in vitro with the construct^{46, 47}. NKG2D-mediated signaling will be assessed by immunoprecipitation of DAP10 or DAP12 followed by Western blotting for phosphotyrosine as previously described^{48, 49}.

Both IL2 and OMCP interact with their cognate receptors with high affinity; the fusion of the two proteins is anticipated to greatly enhance the avidity of the chimeric construct for cells expressing both IL2R and NKG2D. As a consequence, the tethering of the construct to two cell surface receptors may lead to reduced internalization and increased duration of signaling. Combined these two phenomena represent the most likely mechanism for increased proliferation of NK cells in vivo. The signaling via NKG2D relies upon receptor clustering⁴⁵. Since the construct is soluble it is possible, though unlikely, that the chimera will cluster NKG2D and induce DAP10/12 signaling. However, should DAP10/12 signaling be detected, we will then investigate the importance of this signaling in the expansion of NK cells using cells derived from Vav1 knockout mice. Vav1 is a signal mediator downstream of DAP10⁵⁰. Using a Vav1 knockout has the advantage of leaving NKG2D expression intact, in contrast to DAP knockouts⁵⁰. This will remove the NKG2D signaling component while leaving the NKG2D-dependent targeting intact. A clearer understanding of the mechanism of action for OMCP-IL2 chimera dependent expansion will be crucial for further refinements of the therapeutic agent. Understanding these parameters will allow for testing of different construct designs, primarily in the length of the linker between OMCP and IL2, to calibrate the effects of the chimera.

Example 15. In Vivo Immunotherapy with IL2, R38A/F42K IL2 or OMCP Targeted IL2 Constructs

In order to determine if our construct plays a role in immunoregulation of malignancies as well as viral infections we will rely on in vivo models of B16 melanoma and mouse cytomegalovirus (MCMV). In one set of experiments B6 mice will be injected subcutaneously with 1×10⁶ cells of the poorly immunogenic B16 melanoma cell line. One week after tumor injection mice will be divided into 13 groups (5 mice per group) and treated with five daily injections of IL2, R38A/F42K IL2, OMCP fusion constructs or saline as described in FIG. 18 and Table 4. Tumor growth will be followed by daily measurements of diameter for 4 weeks or until one of the groups develops tumors >2 cm in diameter. At that point mice in all groups will be sacrificed for analysis. In addition to tumor growth lymphocyte infiltration of both the tumor and draining inguinal lymph node will be evaluated by flow cytometry. We will quantitate the total number and activation status of CD4⁺Foxp3⁺ T_regs (expressed as % of tumor infiltrating lymphocytes and % ICOS⁺). We will also evaluate NK cell number and activation as measured by IFN-γ production and CD69 upregulation. Tumor apoptosis will be evaluated by TUNEL staining.

TABLE 4
Experimental Design for Dosing for IL2, R38A/F42K IL2,
OMCP-R38A/F42K IL2 or OMCP linked IL2 constructs

	LOW	INTERMEDIATE	HIGH
Dose Cytokine	DOSE	DOSE	DOSE
IL2	Group
1	Group 2	Group 3
R38A/F42K IL2	Group	4	Group 5	Group 6
OMCP-wild-type IL2	Group	7	Group 8	Group 9
OMCP-R38A/F42K	Group	10	Group 11	Group 12
IL2
Saline	Group 13

In order to evaluate the therapeutic potential of IL2 in an infectious disease model, B6 mice will be infected with a sublethal dose of MCMV (5×10⁴) particle forming units (PFUs) as previously described²⁹. Day 1 post infection the mice will be divided into 13 groups (5 mice per group) and treated with five daily injections of IL2, R38A/F42K IL2, OMCP fusion constructs or saline as described in FIG. 18 and Table 4. On post-infection day #6 the mice will be sacrificed and splenic and pulmonary viral load determined by standard plaque assay.

Potential outcomes include a finding that treatment with pure IL2 will have little effect on tumor growth or viral load as we expect to see preferential activation of T_regs over CTLs. We suspect that administration of the mutant R38A/F42K form of IL2 will result a lower tumor and viral burden compared to wild-type IL2 due to less activation of CD4⁺Foxp3⁺ T_regs. Nevertheless it is possible that despite lower levels of T_reg activation the tumor burden will be identical between IL2 and R38A/F42K IL2 due to decreased NK activation by the mutant form of IL2 as well. Potential outcomes include a finding that OMCP IL2 construct-treated mice will have lower tumor burden compared to pure cytokine and predict that OMCP-R38A/F42K IL2 will demonstrate the best efficacy for immunotherapy with the most favorable side effect profile.

If we do not see an effect of OMCP expressing IL2 constructs we will closely evaluate our data for confounding factors such as excessive CTL death due to extreme stimulation as well as possible sequestration of CTLs in systemic organs such as the liver and lungs. If our hypothesis is supported and NK cells are activated and tumor growth ameliorated after OMCP-construct treatment we would repeat these experiments after NK depletion (using anti-NK1.1 clone PK136, mouse anti-mouse depleting antibody) and CD8 depletion (clone YTS169, rat anti-mouse CD8⁺ T cell-depleting antibody) (both from BioXcell, West Lebanon, NH). Based on these results future work will focus on immunotherapy in primary carcinogenesis models.

Example 16. The Effects of IL2, R38A/F42K IL2 or OMCP Targeted IL2 Constructs on Immunosuppression after Radiation Exposure

Sublethal radiation exposure is a constant risk to those involved in combat duty. In addition to the direct carcinogenic effects of radiation-induced DNA damage, sublethal irradiation results in immunologic damage due to selective death of lymphocyte subsets. CD8⁺ T cells and CD44I° naïve T cells are specifically sensitive to radiation-induced death while NK cell function significantly declines after irradiation. CD4⁺25⁺ T cells as well as CD44^hi memory-like T cells, however, have a survival advantage after radiation. Both CD4⁺25⁺ T cells and CD8⁺ CD44^hi T cells can downregulate immune responses, explaining why even limited exposure to radiation can result in significant immunosuppression. Pharmacologic interventions to restore the immune system can alleviate morbidity and mortality of radiation poisoning. Surprisingly the role of IL2 in alleviating radiation-induced changes has never been studied. The low affinity IL2 receptor is expressed on bone marrow-resident hematopoietic stem cells and committed NK progenitors. NK cells, in turn, can secrete granulocyte-macrophage colony-stimulating factor (GM-CSF) upon stimulation, a cytokine that can assist with hematopoietic recovery. Based on these data in this aim we plan to test the hypothesis that IL2 or OMCP-IL2 constructs can assist with hematopoietic recovery after sublethal and lethal irradiation.

Based on previously described models of radiation-induced hematopoietic damage and recovery we will irradiate B6 mice with either sublethal 4.5 or lethal 7.5 Gy from a cesium source. Within one hour of exposure mice in both radiation doses will be randomly divided into 13 groups as described in Table 4 and treated for five days with low, intermediate or high dose IL2, R38A/F42K IL2 or OMCP expressing IL2 constructs (FIG. 18 ). A portion of the mice will be injected with saline after irradiation (group 13) (Table 4) and unirradiated untreated B6 mice will be included as a control as well (group 14). On day 6 hematopoietic recovery will be monitored by flow cytometric analysis of peripheral blood obtained by superficial mandibular vein sampling. The sample will be analyzed for total number of NK cells, T cells, B cells, granulocytes, as well as monocytes and macrophages per ml of blood. Since 90% of untreated mice die 15-25 days after exposure to 7.5 Gy, mice will be followed daily and survival curves in each treatment group will be compared by Kaplan-Meier analysis. Moribund mice in the 7.5 Gy group will be carefully analyzed for cause of death evaluating the bone marrow, spleen and peripheral organs for both infection as well as hematopoietic failure by flow cytometry and tissue culture. Since mice in the sublethal 4.5 Gy group are expected to survive long term, they will be sacrificed one month after exposure and peripheral lymphoid organs as well as bone marrow evaluated for hematopoietic recovery by flow cytometric analysis.

Radiation related DNA damage results in malignant transformation. Hematopoietic malignancies are especially prominent after radiation exposure. In order to evaluate the ability of IL2 or OMCP linked IL2 constructs to facilitate in clearing hematopoietic malignancies after radiation exposure we will treat B6 mice with sublethal exposure to 4.5 Gy from a cesium source. Two days after irradiation the mice will be injected with 10³ RMA-S lymphoma cells i.p. and three days later treated for a five day course with low, intermediate or high dose IL2, R38A/F42K IL2 or OMCP expressing IL2 constructs (Table 4, FIG. 19 ). Unirradiated B6 mice will be included as a control (group 14) as well. The mice will be followed for survival.

We anticipate that wild-type IL2 alone will have a negligible effect on immunorestoration since it will most likely result in preferential expansion of CD4⁺Foxp3⁺ T_regs, which are already preserved after irradiation. We suspect, however, that R38A/F42K IL2 as well as OMCP expressing IL2 constructs will expand the NK fraction in the peripheral blood and will contribute to broad hematopoietic recovery, albeit indirectly through secretion of homeostatic cytokines such as GM-CSF. If we detect no differences in hematopoietic recovery between IL2 and saline-treated groups, we will examine other confounding factors, such as homeostatic proliferation induced alteration of the immune system and the effect of IL2 or OMCP expressing IL2 constructs on such proliferation. While 200,000 IU of IL2 administered daily to B6 mice is not lethal, we realize that in the face of irradiation the mice might be weaker. It is thus possible that dosing might need to be adjusted. For the “functional” part of this experiment we plan to specifically utilize the well-established model of RMA-S lymphoma challenge due to the role of NK cells in controlling hematologic malignancies. This established assay will allow us to gain rapid experimental data to advance this aim. Based on this data we would extend this aim in the future utilizing a primary carcinogenesis model as well.

Example 17. OMCP-Targeted Delivery of IL15 Enhances CD25 Upregulation

Interleukin 15 (IL15) is a cytokine with structural similarity to IL2. Like IL2, IL15 binds to and signals through a complex composed of IL2/IL15 receptor beta chain (CD122) and the common gamma chain (gamma-C, CD132). IL15 is secreted by mononuclear phagocytes (and some other cells) following infection by viruses. IL15 regulates T and natural killer (NK) cell activation and proliferation. Survival signals that maintain memory T cells in the absence of antigen are provided by IL15. This cytokine is also implicated in NK cell development. IL-15 belongs to the four α-helix bundle family of cytokine.

OMCP was linked to the cytokine IL15 and its ability to active NK cells compared to IL15 alone was examined. NK cell activation was measured by CD25 upregulation. As demonstrated in FIG. 21 , higher levels of CD25 are evident when IL15 is delivered by OMCP vs naked cytokine alone in equimolar doses.

Example 18. OMCP-Targeted Delivery of IL18 Enhances NK Cell Activation

OMCP was linked to WT human IL18, WT murine IL18 or mutant human IL18 (which inhibits its interaction with IL18BP) and its ability to active NK cells was examined (FIG. 32 ). Peripheral blood lymphocytes were cultured for 48 hours in 4.4 μM of either wild-type IL18 (blue), OMCP-IL18 (red) or saline (black). Activation of CD56+CD3− natural killer cells, as measured by surface CD69 expression, was superior by OMCP-IL18 compared to wild-type IL18 (FIG. 33 ). This data demonstrates that linking OMCP to IL18 also enhances NK cell activation relative to IL18 without OMCP.

Example 19. The D132R Mutation in OMCP Significantly Decreases its NKG2D Binding

To further test the necessity of NKG2D binding in targeted delivery of IL2, we tested NK expansion and activation in the presence of mutIL2, OMCP-mutIL2, and (D132R) OMCP-mutIL2. The D132R mutation ameliorated the superiority of natural killer cell activation over cytokine alone (FIG. 22 ). Thus high affinity NKG2D binding is critical for targeted delivery and lymphocyte activation by IL2.

Example 20. OMCP-IL2 Effectively Treats Infection Caused by West Nile Virus (WNV)

The ability of various constructs of the invention to treat infection caused by West Nile Virus (WNV) was evaluated. Mice were given OMCP-IL2, the binding null mutant of OMCP, OMCP(D132R)-IL2, IL2 alone, IL2(38R/42A) alone and PBS. Upon treatment with OMCP(D132R)-IL2 and PBS all mice succumbed to infection by about day 11. Following treatment with IL2 alone, approximately 20% of mice survived until day 21. However, treatment with IL2(38R/42A) and OMCP-IL2 resulted in about 40% of mice surviving beyond 21 days (FIG. 30A). These results were consistently repeatable as demonstrated in FIG. 30B.

REFERENCES FOR EXAMPLE 11-20

• 1. Rosenberg, S. A. IL2: the first effective immunotherapy for human cancer. J Immunol 192, 5451-5458 (2014).
• 2. Atkins, M. B., et al. High-dose recombinant interleukin 2 therapy for patients with metastatic melanoma: analysis of 270 patients treated between 1985 and 1993. J Clin Oncol 17, 2105-2116 (1999).
• 3. Krieg, C., Letourneau, S., Pantaleo, G. & Boyman, O. Improved IL2 immunotherapy by selective stimulation of IL2 receptors on lymphocytes and endothelial cells. Proc Natl Acad Sci USA 107, 11906-11911 (2010).
• 4. Ghiringhelli, F., Menard, C., Martin, F. & Zitvogel, L. The role of regulatory T cells in the control of natural killer cells: relevance during tumor progression. Immunol Rev 214, 229-238 (2006).
• 5. French, A. R., et al. DAP12 signaling directly augments proproliferative cytokine stimulation of NK cells during viral infections. J Immunol 177, 4981-4990 (2006).
• 6. Heaton, K. M., Ju, G. & Grimm, E. A. Human interleukin 2 analogues that preferentially bind the intermediate-affinity interleukin 2 receptor lead to reduced secondary cytokine secretion: implications for the use of these interleukin 2 analogues in cancer immunotherapy. Cancer Res 53, 2597-2602 (1993).
• 7. Heaton, K. M., et al. Characterization of lymphokine-activated killing by human peripheral blood mononuclear cells stimulated with interleukin 2 (IL2) analogs specific for the intermediate affinity IL2 receptor. Cellular immunology 147, 167-179 (1993).
• 8. Levin, A. M., et al. Exploiting a natural conformational switch to engineer an interleukin-2 ‘superkine’. Nature 484, 529-533 (2012).
• 9. Campbell, J. A., Trossman, D. S., Yokoyama, W. M. & Carayannopoulos, L. N. Zoonotic orthopoxviruses encode a high-affinity antagonist of NKG2D. J Exp Med 204, 1311-1317 (2007).
• 10. Rosenberg, S. A., et al. Experience with the use of high-dose interleukin-2 in the treatment of 652 cancer patients. Annals of surgery 210, 474-484; discussion 484-475 (1989).
• 11. Gately, M. K., Anderson, T. D. & Hayes, T. J. Role of asialo-GM1-positive lymphoid cells in mediating the toxic effects of recombinant IL2 in mice. J Immunol 141, 189-200 (1988).
• 12. Sim, G. C., et al. IL2 therapy promotes suppressive ICOS⁺ Treg expansion in melanoma patients. J Clin Invest 124, 99-110 (2014).
• 13. Raulet, D. H. Roles of the NKG2D immunoreceptor and its ligands. Nat Rev Immunol 3, 781-790 (2003).
• 14. Ullrich, E., Koch, J., Cerwenka, A. & Steinle, A. New prospects on the NKG2D/NKG2DL system for oncology. Oncoimmunology 2, e26097 (2013).
• 15. Lazear, E., Peterson, L. W., Nelson, C. A. & Fremont, D. H. Crystal structure of the cowpox virus-encoded NKG2D ligand OMCP. J Virol 87, 840-850 (2013).
• 16. Bui, J. D., Uppaluri, R., Hsieh, C. S. & Schreiber, R. D. Comparative analysis of regulatory and effector T cells in progressively growing versus rejecting tumors of similar origins. Cancer Res 66, 7301-7309 (2006).
• 17. Wang, Y., Sparwasser, T., Figlin, R. & Kim, H. L. Foxp3+ T cells inhibit antitumor immune memory modulated by mTOR inhibition. Cancer Res 74, 2217-2228 (2014).
• 18. Poschke, I., et al. A phase I clinical trial combining dendritic cell vaccination with adoptive T cell transfer in patients with stage IV melanoma. Cancer immunology, immunotherapy: CII 63, 1061-1071 (2014).
• 19. Kreisel, D., et al. Strain-specific variation in murine natural killer gene complex contributes to differences in immunosurveillance for urethane-induced lung cancer. Cancer Res 72, 4311-4317 (2012).
• 20. Frese-Schaper, M., et al. Influence of natural killer cells and perforinmediated cytolysis on the development of chemically induced lung cancer in NJ mice. Cancer immunology, immunotherapy: CII 63, 571-580 (2014).
• 21. Ryu, M. S., et al. Accumulation of cytolytic CD8(+) T cells in B16-melanoma and proliferation of mature T cells in TIS21-knockout mice after T cell receptor stimulation. Experimental cell research 327, 209221 (2014).
• 22. Anichini, A., et al. Tumor-reactive CD8⁺ early effector T cells identified at tumor site in primary and metastatic melanoma. Cancer Res 70, 8378-8387 (2010).
• 23. Glasner, A., et al. Recognition and prevention of tumor metastasis by the NK receptor NKp46/NCR1. J Immunol 188, 2509-2515 (2012).
• 24. Hersey, P., Edwards, A., Honeyman, M. & McCarthy, W. H. Low natural-killer-cell activity in familial melanoma patients and their relatives. Br J Cancer 40, 113-122 (1979).
• 25. Ji, Q., Gondek, D. & Hurwitz, A. A. Provision of granulocyte-macrophage colony-stimulating factor converts an autoimmune response to a self-antigen into an antitumor response. J Immunol 175, 14561463 (2005).
• 26. Zhu, Z., et al. High-avidity T cells are preferentially tolerized in the tumor microenvironment. Cancer Res 73, 595-604 (2013).
• 27. Klein, O., et al. Melan-A-specific cytotoxic T cells are associated with tumor regression and autoimmunity following treatment with anti-CTLA-4. Clinical cancer research: an official journal of the American Association for Cancer Research 15, 2507-2513 (2009).
• 28. Meiraz, A., Garber, O. G., Harari, S., Hassin, D. & Berke, G. Switch from perforin-expressing to perforin-deficient CD8(+) T cells accounts for two distinct types of effector cytotoxic T lymphocytes in vivo. Immunology 128, 69-82 (2009).
• 29. Stemberger, C., et al. A single naive CD8⁺ T cell precursor can develop into diverse effector and memory subsets. Immunity 27, 985-997 (2007).
• 30. Sallusto, F., Lenig, D., Forster, R., Lipp, M. & Lanzavecchia, A. Two subsets of memory T lymphocytes with distinct homing potentials and effector functions. Nature 401, 708-712 (1999).
• 31. Araki, K., et al. mTOR regulates memory CD8 T-cell differentiation. Nature 460, 108-112 (2009).
• 32. Kim, H. L. Antibody-based depletion of Foxp3+ T cells potentiates antitumor immune memory stimulated by mTOR inhibition. Oncoimmunology 3, e29081 (2014).
• 33. Graham, J. B., Da Costa, A. & Lund, J. M. Regulatory T cells shape the resident memory T cell response to virus infection in the tissues. J Immunol 192, 683-690 (2014).
• 34. de Goer de Herve, M. G., Jaafoura, S., Vallee, M. & Taoufik, Y. FoxP3(+) regulatory CD4 T cells control the generation of functional CD8 memory. Nature communications 3, 986 (2012).
• 35. Gilfillan, S., Ho, E. L., Cella, M., Yokoyama, W. M. & Colonna, M. NKG2D recruits two distinct adapters to trigger NK cell activation and costimulation. Nature immunology 3, 1150-1155 (2002).
• 36. Shane, H. L. & Klonowski, K. D. Every breath you take: the impact of environment on resident memory CD8 T cells in the lung. Frontiers in immunology 5, 320 (2014).
• 37. Marcus, A. & Raulet, D. H. Evidence for natural killer cell memory. Current biology: CB 23, R817-820 (2013).
• 38. Tam, S. H., Sassoli, P. M., Jordan, R. E. & Nakada, M. T. Abciximab (ReoPro, chimeric 7E3 Fab) demonstrates equivalent affinity and functional blockade of glycoprotein IIb/IIIa and alpha(v)beta3 integrins. Circulation 98, 1085-1091 (1998).
• 39. Trikha, M., et al. CNTO 95, a fully human monoclonal antibody that inhibits alphav integrins, has antitumor and antiangiogenic activity in vivo. International journal of cancer. Journal international du cancer 110, 326-335 (2004).
• 40. Rathanaswami, P., Babcook, J. & Gallo, M. High-affinity binding measurements of antibodies to cell-surface-expressed antigens. Anal Biochem 373, 52-60 (2008).
• 41. Drake, A. W., Myszka, D. G. & Klakamp, S. L. Characterizing high-affinity antigen/antibody complexes by kinetic- and equilibrium-based methods. Anal Biochem 328, 35-43 (2004).
• 42. Siiman, 0. & Burshteyn, A. Cell surface receptor-antibody association constants and enumeration of receptor sites for monoclonal antibodies. Cytometry 40, 316-326 (2000).
• 43. Debbia, M. & Lambin, P. Measurement of anti-D intrinsic affinity with unlabeled antibodies. Transfusion 44, 399-406 (2004).
• 44. Tsao, P. I. & von Zastrow, M. Type-specific sorting of G protein-coupled receptors after endocytosis. The Journal of biological chemistry 275, 11130-11140 (2000).
• 45. Lazear, E., et al. Cowpox virus OMCP antagonizes NKG2D via an unexpected binding orientation. PLos Pathogen Under review(2014).
• 46. Liu, K. D., Gaffen, S. L., Goldsmith, M. A. & Greene, W. C. Janus kinases in interleukin-2-mediated signaling: JAK1 and JAK3 are differentially regulated by tyrosine phosphorylation. Current biology: CB 7, 817-826 (1997).
• 47. Zhou, Y. J., et al. Distinct tyrosine phosphorylation sites in JAK3 kinase domain positively and negatively regulate its enzymatic activity. Proc Natl Acad Sci USA 94, 13850-13855 (1997).
• 48. Horng, T., Bezbradica, J. S. & Medzhitov, R. NKG2D signaling is coupled to the interleukin 15 receptor signaling pathway. Nature immunology 8, 1345-1352 (2007).
• 49. Zou, W., Reeve, J. L., Liu, Y., Teitelbaum, S. L. & Ross, F. P. DAP12 couples c-Fms activation to the osteoclast cytoskeleton by recruitment of Syk. Molecular cell 31, 422-431 (2008).
• 50. Graham, D. B., et al. Vav1 controls DAP10-mediated natural cytotoxicity by regulating actin and microtubule dynamics. J Immunol 177, 2349-2355 (2006).
• 51. Yamane, B. H., Hank, J. A., Albertini, M. R. & Sondel, P. M. The development of antibody-IL2 based immunotherapy with hu14.18-IL2 (EMD-273063) in melanoma and neuroblastoma. Expert opinion on investigational drugs 18, 991-1000 (2009).
• 52. Becker, J. C., Pancook, J. D., Gillies, S. D., Furukawa, K. & Reisfeld, R. A. T cell-mediated eradication of murine metastatic melanoma induced by targeted interleukin 2 therapy. J Exp Med 183, 2361-2366 (1996).
• 53. Lundholm et al., Prostate tumor-derived exosomes down-regulate NKG2D expression on natural killer cells and CD8⁺ T cells: mechanism of immune evasion. PLoS One 2014; 9(9):e108925.

Example 21. Anti-NKG2D Antibody-Mediated Delivery of R38A/F42K Mutant IL-2

In order to compare antibody-mediated delivery of mutIL-2 to OMCP-mediated delivery of mutIL-2, 4 anti-human NKG2D single chain variable fragment domains were engineered based on the described sequence of the KYK1 and KYK2 antibodies (J Mol Biol 2008, 384(5), 1143-1156). 1HL2 and are 1LH2 derived from the kyk1 antibody and 2HL2 and 2LH2 from the kyk2 antibody. The binding coefficients of OMCP, KYK1 and KYK2 are 0.1 nM, 27 nM and 6 nM, respectively.

Antibodies linked to OMCP-mutant IL-2, IgG-mutant IL-2, wild type IL-2 and PBS control were co-cultured with 2.5×10⁶ peripheral blood lymphocytes in 500 μl of media in either 10 U/ml or 100 U/ml final concentration of cytokine or construct. Forty-eight hours later NK activation was evaluated as relative median fluorescence intensity of intracellular perforin compared to PBS control. CD4⁺CD45RA⁻Foxp3⁺ activation was evaluated as relative median fluorescence intensity of surface CD25 compared to PBS control.

At 10 U/ml OMCP-mutant IL-2 demonstrated a trend toward increased perforin levels over antibody-mediated delivery but it did not reach statistical significance (FIG. 39 ). At 100 U/ml NK cells treated with 2HL2 and 2LH2 antibodies synthesized as much perforin as OMCP-mutIL-2 treated cells but lower levels of perforin were evident in 1HL2 and 1LH2 treated NK cells. Higher levels of CD25 were evident in wild-type IL-2 treated cultures over all constructs. Accordingly, the results demonstrate that mutant IL-2 linked to NKG2D antibodies performs comparably to OMCP linked to mutant IL-2.

Example 22. Combination Therapy with an OMCP-IL2 and PD-1 Inhibitor

This example describes in vivo testing of combination therapies of OMCP-IL2 in combination with a PD-1 antibody.

A total of 16 C57131/6 mice 6-9 weeks of age were seeded with 100,000 Lewis Lung Carcinoma cells per mouse via tail vein injection to induce seeding of the tumor cells into the lungs. Mice were subsequently randomized into four groups to receive the following therapies, which were initiated 5 days post-cell seeding:

• • Group 1—antibody isotype control,
  • Group 2—anti-PD-1 antibody therapy,
  • Group 3—antibody isotype control plus OMCP-IL2,
  • Group 4—anti-PD-1 antibody plus OMCP-IL2.
  • Group 1—The mice were intraperitoneally (i.p.) administered 250 μg isotype control antibody (Bioxcell clone no. 2A3, cat no. BP0089) twice weekly for two weeks for a total of 4 doses (1000 μg total) of antibody.
  • Group 2—The mice were administered i.p. 250 μg of an anti-PD-1 antibody (Bioxcell clone no. RMP1-14, cat. no. BP0146) twice weekly for two weeks for a total of 4 doses (1000 μg total) of antibody.
  • Group 3—The mice were administered i.p. (i) 75,000 IUe OMCP-IL2 fusion protein twice daily for five days for a total of ten doses (750,000 IUe) of OMCP-IL2 fusion protein; and (ii) 250 μg isotype control antibody (Bioxcell clone no. 2A3, cat no. BP0089) twice weekly for two weeks for a total of 4 doses (1000 μg total) of antibody.
  • Group 4—The mice were administered i.p. (i) 75,000 IUe OMCP-IL2 fusion protein twice daily for five days for a total of ten doses (750,000 IUe) of OMCP-IL2 fusion protein; and (ii) 250 μg of an anti-PD-1 antibody (Bioxcell clone no. RMP1-14, cat. no. BP0146) twice weekly for two weeks for a total of 4 doses (1000 μg total) of antibody.

Mice were retained for three weeks after the completion of the respective therapy, at which time they were euthanized.

Because tumor burden measurably increases the weight of the lungs, lung weight was used as a primary measurement for therapy efficacy. FIG. 34 depicts photographs of lungs of the Groups 1-4 mice cohorts and FIG. 35 depicts lung weights as measured from the lungs from the Group 1-4 mice cohorts. As shown in FIGS. 34 and 35 , the combination of an anti-PD-1 antibody and OMCP-IL2 (Group 4) was found to virtually eliminate tumor growth in the lung, and synergistically decreases tumor burden over either OMCP-IL2 therapy alone (Group 3) or anti-PD-1 antibody therapy alone (Group 2). Thus, the combination therapy demonstrated surprisingly greater efficacy than each component administered alone.

Example 23. PD1-Targeted Delivery of an IL2 Mutant Preferentially Activates Cytotoxic Lymphocytes In Vitro

This example describes in vitro testing of PD1 ligand therapies. Specifically, this example will demonstrate improved immune cell activation of PDL1-mutIL2 and PDL2-mutIL2 fusion proteins over purified cytokine.

A total of 4 C57131/6 mice 6-9 weeks of age will be utilized to prepare a fresh splenocyte culture. Splenocytes will be cultured in triplicate for 36 hours according to the following groups: Group 1—saline control, Group 2—100 IUe/mL wt IL2, Group 3—100 IUe/mL mut IL2, Group 4—100 IUe/mL PDL1, Group 5—100 IUe/mL PDL2, Group 6—100 IUe/mL PDL1-mutIL2, Group 7—100 IUe/mL PDL2-mutIL2. After the 36-hour culture period, cells will be stained for flow cytometry according to standard protocols, and cellular activation will be evaluated.

Cellular populations will be defined via the following gating strategies: T_regs—CD45+CD3+CD4+Foxp3+, NK cells—CD45+CD3−CD49b+CD335+, Teff—CD45+CD3+CD8⁺. Cellular activation will be further defined via evaluation whether the following markers are upergulated: T_regs—ICOS, NK cells—CD69 and KLRG1, Teff—CD69.

Potential outcomes include a finding that NK cells are significantly activated by treatment with wtIL2, PDL1-mutIL2, and PDL2-mutIL2. Teff cells may also be activated by treatment with wtIL2, PDL1-mutIL2, and PDL2-mutIL2. This is in contrast with T_regs, which should be activated by treatment with wtIL2 but not with PDL1-mutIL2 or PDL2-mutIL2.

These results would suggest that targeting IL2 therapy to PD1 cells via a PD1 ligand fusion protein significantly enhances the efficacy of IL2 therapy in anti-tumor cell populations such as NK cells and Teff cells, while avoiding activation of immunotolerant populations such as Treg cells.

Example 24. PD1-Targeted Delivery of an IL2 Mutant Induces Proliferation of Cytotoxic Lymphocytes In Vitro

This example describes in vitro testing of PD1 ligand therapies. Specifically, this example will demonstrate improved cytotoxic immune cell expansion by PDL1-mutIL2 and PDL2-mutIL2 fusion proteins over purified cytokine.

A total of 4 C57Bl/6 mice 6-9 weeks of age will be utilized to prepare a fresh splenocyte culture. Splenocytes will be stained with CFSE prior to culture. CFSE permanently binds DNA, and provides an indication of cellular proliferation via reduced fluorescence with subsequent cellular divisions. Stained splenocytes will be subsequently cultured in triplicate for 6 days according to the following groups: Group 1 saline control, Group 2—1000 IUe/mL wt IL2, Group 3—1000 IUe/mL mut IL2, Group 4—1000 IUe/mL PDL1, Group 5—1000 IUe/mL PDL2, Group 6—1000 IUe/mL PDL1-mutIL2, Group 7—1000 IUe/mL PDL2-mutIL2. After the 6-day culture period, cells will be stained for flow cytometry according to standard protocols, and cellular proliferation will be evaluated.

Cellular populations will be defined via the following gating strategies: T_regs—CD45+CD3+CD4+Foxp3+, NK cells—CD45+CD3−CD49b+CD335+, Teff—CD45+CD3+CD8+.

Potential outcomes include a finding that wtIL2, PDL1-mutIL2, and PDL2-mutIL2 will induce significant proliferation in the NK cell population. We may also find that Teff cells are induced to proliferate via these same treatment groups. However, Treg cells will only be induced to proliferate by the wtIL2 treatment, and will remain relatively quiescent with PDL1-mutIL2 and PDL2-mutIL2 treatment. Therefore, the NK cell to Treg cell ratio, a marker for immune cell activation and prognostic for cancer therapeutic responses, will be significantly enhanced by PDL1-mutIL2 and PDL2-mutIL2 treatment over the wtIL2 treatment alone.

These results would suggest that targeting IL2 therapy to PD1 cells via a PD1 ligand fusion protein significantly enhances the proliferative capacity of anti-tumor cell populations such as NK cells and Teff cells, while avoiding activation of immunotolerant populations such as Treg cells.

Example 25. Lymphocyte Cytotoxicity is Enhanced by PD1 Targeted Delivery of Mutant IL2

This example describes in vitro testing of PD1 ligand therapies. Specifically, this example will demonstrate improved cytotoxic immune cell response after treatment with PDL1-mutIL2 and PDL2-mutIL2 fusion proteins over purified cytokine.

A total of 6 C57131/6 mice 6-9 weeks of age will be utilized to prepare a fresh splenocyte culture. Bulk splenocytes will be cultured for 6 days according to the following groups: Group 1—saline control, Group 2—1000 IUe/mL wt IL2, Group 3—1000 IUe/mL mut IL2, Group 4—1000 IUe/mL PDL1, Group 5—1000 IUe/mL PDL2, Group 6—1000 IUe/mL PDL1-mutIL2, Group 7—1000 IUe/mL PDL2-mutIL2. After the 6-day culture period, cells will be prepared for a 7-AAD/CFSE cytotoxicity assay against K562 cells using a kit according to the manufacturer's protocols (Cayman Chemical, 7-AAD/CFSE Cell-Mediated Cytotoxicity Assay Kit, Item No. 600120). Splenocytes from each group will be seeded with target K562 cells in triplicate at the following ratios: no target cells, 15.6:1, 31.25:1, 62.5:1, 125:1, 250:1, 500:1. After 4 hours, the live versus dead target cell ratio will be evaluated via flow cytometry.

Potential outcomes include a finding that splenocytes incubated with wtIL2 will have enhanced cytotoxic function against the target cells versus saline controls. We further expect to find that PDL1-mutIL2 and PDL2-mutIL2 treatment will further enhance the cytotoxicity of the splenocytes.

These results would suggest that PD1 ligand IL2 fusion proteins increase splenocyte cytotoxic activity over wtIL2 therapy. This may be a function of decreased Treg activation within the splenocyte population. This may further be a function of enhanced binding and signaling of the mutIL2 portion of the fusion proteins through the IL2 receptor on T and NK cells.

Example 26. Tumor Growth and Survival after In Vivo Treatment with PD1 Targeted Therapies

This example describes in vivo proof of concept that PD1 ligand therapies inhibit tumor or cancer progression. Specifically, this example will demonstrate improved tumor growth and overall survival metrics after in vivo treatment with PDL1-mutIL2 and PDL2-mutIL2 fusion proteins over purified cytokine.

A total of 50 C57Bl/6 mice 6-9 weeks of age will be utilized. Mice will be injected with Lewis Lung Carcinoma subcutaneously at the flank with 1×105 cells per mouse. Treatment will begin 5 days later, when tumors have grown sufficiently to become visible and measurable. Initial tumor sizes and mouse weights will be taken, and mice will be randomized into groups of 10 mice such that the initial tumor sizes and mouse weights are similar between groups. The treatment groups are as follows: Group 1—saline control, Group 2—wt IL2, Group 3—mut IL2, Group 4—PDL1-mutIL2, Group 5—PDL2-mutIL2.

All mice will be treated according to their groups twice daily in 12 hour intervals for 5 days, a total of 10 doses. Group 1—The mice will be intraperitoneally (i.p.) administered 200 μL saline for all treatments as a negative control. Group 2—The mice will be i.p. administered 75,000 IUe wt IL2 for each dose, for a total of 750,000 IUe wt IL2 after treatment. Group 3—The mice will be i.p. administered 75,000 IUe mut IL2 for each dose, for a total of 750,000 IUe mut IL2 after treatment. Group 4—The mice will be i.p. administered 75,000 IUe PDL1-mutIL2 for each dose, for a total of 750,000 IUe PDL1-mutIL2 after treatment. Group 5—The mice will be i.p. administered 75,000 IUe PDL2-mutIL2 for each dose, for a total of 750,000 IUe PDL2-mutIL2 after treatment.

All tumors will be measured via caliper measurements and mouse weights measured every day during treatment. After the completion of the therapeutic course, mouse weights and tumors will be measured thrice weekly. Mice will be monitored throughout the study for signs of distress or other effects of the therapeutic treatment All mice will be euthanized at a maximum tumor diameter of 20 mm, and tumors will be reserved for later analysis. Any mice that die prematurely from known or unknown causes will have a final measurement taken and tissues collected as soon as is possible.

Potential outcomes include a finding that mice treated with wt IL2 will exhibit considerable physiological distress compared to saline controls, and may even die prematurely from the treatment itself due to vascular leak syndrome (VLS). Those mice that survive the treatment may have some attenuated tumor growth and increased survival compared to saline controls. Potential outcomes further include a finding that mice treated with mut IL2 will not have VLS and the associated physiological stresses, but will have little or no attenuation of tumor growth compared with the saline control mice. In comparison, potential outcomes may include a finding that treatment with PDL1-mutIL2 and PDL2-mutIL2 will significantly attenuate tumor growth and increase survival over both the saline control and the wt IL2 group.

We will further analyze residual tumors for lymphocyte infiltration via immunohistochemistry. Specifically, we will evaluate the intratumoral infiltration of CD8+ Teff cells and NK cells. Further, we will evaluate the apoptotic levels via a TUNEL assay (Millipore ApopTag Peroxidase In Situ Apoptosis Detection Kit, Cat No. S7100). Potential outcomes include a finding that treatment with PDL1-mutIL2 and PDL2-mutIL2 increases CD8⁺ Teff an NK cell intratumoral infiltration significantly over either saline control mice or wt IL2 treated mice.

These results would suggest that PD1 ligand IL2 fusion proteins, specifically PDL1-mutIL2 and PDL2-mutIL2, have an increased therapeutic benefit as compared to wt IL2 or mut IL2 cytokine treatment alone. By targeting the IL2 treatment to PD1 expressing cells, unintended toxicities and side effects will be reduced as compared to wt IL2 treatment. Further, intratumoral infiltration of cytotoxic lymphocytes is enhanced by the PD1 ligand IL2 fusion proteins, suggesting that targeted activation of these cellular populations increases the capacity of these cells to overcome the immunosuppression of the tumor cells.

Example 27. NKG2D Targeted Delivery of OX40L Preferentially Activates Cytotoxic Lymphocytes In Vitro

This example describes in vitro testing of NKG2D targeted delivery of OX40L therapies. Specifically, this example will demonstrate improved immune cell activation of OMCP-OX40L over purified cytokine. This example will further demonstrate inhibition of OX40L signaling by OMCP-OX40L mutt and OMCP-OX40L mut2.

A total of 4 C57Bl/6 mice 6-9 weeks of age will be utilized to prepare a fresh splenocyte culture. Splenocytes will be cultured in triplicate for 36 hours according to the following groups: Group 1—saline control, Group 2—100 IUe/mL OX40L, Group 3—100 IUe/mL OX40L mut1, Group 4—100 IUe/mL OX40L mut2, Group 5—100 IUe/mL OMCP-OX40L, Group 6—100 IUe/mL OMCP-OX40L mutt, Group 7—100 IUe/mL OMCP-OX40L mut2. After the 36-hour culture period, cells will be stained for flow cytometry according to standard protocols, and cellular activation will be evaluated.

Cellular populations will be defined via the following gating strategies: T_regs—CD45+CD3+CD4+Foxp3+, NK cells—CD45+CD3−CD49b+CD335+, Teff—CD45+CD3+CD8+. Cellular activation will be further defined via evaluation whether the following markers are upergulated: T_regs—ICOS, NK cells—CD69 and KLRG1, Teff—CD69.

Potential outcomes include a finding that NK cells are significantly activated by treatment with OX40L and OMCP-OX40L. Teff cells may also be activated by treatment with OX40L, and OMCP-OX40L. This is in contrast with OX40L mutt, OX40L mut2, OMCP-OX40L mutt, and OMCP-OX40L mut2, which should inhibit NK cell activation. Further, Teff cells may also be inhibited by treatment with OX40L mutt, OX40L mut2, OMCP-OX40L mutt, and OMCP-OX40L mut2, which should inhibit NK cell activation.

These results would suggest that targeting OX40L therapy to NKG2D expressing cells via OMCP ligand fusion protein significantly enhances the efficacy of OX40L therapy in anti-tumor cell populations such as NK cells and Teff cells.

Example 28. NKG2D Targeted Delivery of OX40L Induces Proliferation of Cytotoxic Lymphocytes In Vitro

This example describes in vitro testing of NKG2D targeted delivery of OX40L therapies. Specifically, this example will demonstrate improved cytotoxic immune cell expansion by OMCP-OX40L over purified cytokine.

A total of 4 C57Bl/6 mice 6-9 weeks of age will be utilized to prepare a fresh splenocyte culture. Splenocytes will be stained with CFSE prior to culture. CFSE permanently binds DNA, and provides an indication of cellular proliferation via reduced fluorescence with subsequent cellular divisions. Stained splenocytes will be subsequently cultured in triplicate for 6 days according to the following groups: Group 1—saline control, Group 2—1000 IUe/mL OX40L, Group 3—1000 IUe/mL OX40L mutt, Group 4—1000 IUe/mL OX40L mut2, Group 5—1000 IUe/mL OMCP-OX40L, Group 6—1000 IUe/mL OMCP-OX40L mutt, Group 7—1000 IUe/mL OMCP-OX40L mut2. After the 6-day culture period, cells will be stained for flow cytometry according to standard protocols, and cellular proliferation will be evaluated.

Cellular populations will be defined via the following gating strategies: T_regs—CD45+CD3+CD4+Foxp3+, NK cells—CD45+CD3−CD49b+CD335+, Teff—CD45+CD3+CD8+.

Potential outcomes include a finding that OX40L and OMCP-OX40L will induce significant proliferation in the NK cell population. We may also find that Teff cells are induced to proliferate via these same treatment groups. However, potential outcomes may include a finding that treatment with OX40L mutt, OX40L mut2, OMCP-OX40L mutt, and OMCP-OX40L mut2 will not induce either NK cell or Teff cell expansion. The NK cell to Treg cell ratio, a marker for immune cell activation and prognostic for cancer therapeutic responses, will be significantly enhanced by OMCP-OX40L treatment over the OX40L treatment alone.

These results would suggest that targeting OX40L therapy to NKG2D expressing cells via a NKG2D ligand fusion protein significantly enhances the proliferative capacity of anti-tumor cell populations such as NK cells and Teff cells.

Example 29. Lymphocyte Cytotoxicity is Enhanced by NKG2D Targeted Delivery of OX40L

This example describes in vitro testing of NKG2D targeted delivery of OX40L therapies. Specifically, this example will demonstrate improved cytotoxic immune cell response after treatment with OMCP-OX40L over purified cytokine.

A total of 6 C57131/6 mice 6-9 weeks of age will be utilized to prepare a fresh splenocyte culture. Bulk splenocytes will be cultured for 6 days according to the following groups: Group 1—saline control, Group 2—1000 IUe/mL OX40L, Group 3—1000 IUe/mL OX40L mutt, Group 4—1000 IUe/mL OX40L mut2, Group 5—1000 IUe/mL OMCP-OX40L, Group 6—1000 IUe/mL OMCP-OX40L mutt, Group 7—1000 IUe/mL OMCP-OX40L mut2. After the 6-day culture period, cells will be prepared for a 7-AAD/CFSE cytotoxicity assay against K562 cells using a kit according to the manufacturer's protocols (Cayman Chemical, 7-AAD/CFSE Cell-Mediated Cytotoxicity Assay Kit, Item No. 600120). Splenocytes from each group will be seeded with target K562 cells in triplicate at the following ratios: no target cells, 15.6:1, 31.25:1, 62.5:1, 125:1, 250:1, 500:1. After 4 hours, the live versus dead target cell ratio will be evaluated via flow cytometry.

Potential outcomes include a finding that splenocytes incubated with OX40L, will have enhanced cytotoxic function against the target cells versus saline, OX40L mutt, and OX40L mut2 controls. Potential outcomes further include a finding that OMCP-OX40L treatment will further enhance the cytotoxicity of the splenocytes.

These results would suggest that NKG2D ligand OX40L fusion proteins increase splenocyte cytotoxic activity over OX40L therapy. This may be a function of enhanced binding and signaling of the OX40L portion of the fusion proteins through the OX40 receptor on T and NK cells.

Example 30. Tumor Growth and Survival after In Vivo Treatment with OMCP-OX40L Targeted Therapies

This example describes in vivo proof of concept that OMCP-OX40L therapies inhibit tumor or cancer progression. Specifically, this example will demonstrate improved tumor growth and overall survival metrics after in vivo treatment with OMCP-OX40L fusion proteins over purified cytokine.

A total of 70 C57Bl/6 mice 6-9 weeks of age will be utilized. Mice will be injected with Lewis Lung Carcinoma subcutaneously at the flank with 1×105 cells per mouse. Treatment will begin 5 days later, when tumors have grown sufficiently to become visible and measurable. Initial tumor sizes and mouse weights will be taken, and mice will be randomized into groups of 10 mice such that the initial tumor sizes and mouse weights are similar between groups. The treatment groups are as follows: Group 1—saline control, Group 2—OX40L, Group 3—OX40L mutt, Group 4—OX40L mut2, Group 5—OMCP-OX40L, Group 6—OMCP-OX40L mutt, Group 7—OMCP-OX40L mut2.

All mice will be treated according to their groups twice daily in 12 hour intervals for 5 days, a total of 10 doses. Group 1—The mice will be intraperitoneally (i.p.) administered 200 μL saline for all treatments as a negative control. Group 2—The mice will be i.p. administered 75,000 IUe OX40L for each dose, for a total of 750,000 IUe OX40L after treatment. Group 3—The mice will be i.p. administered 75,000 IUe OX40L mut 1 for each dose, for a total of 750,000 IUe OX40L mut 1 after treatment. Group 4—The mice will be i.p. administered 75,000 IUe OX40L mut 2 for each dose, for a total of 750,000 IUe OX40L mut 2 after treatment. Group 5—The mice will be i.p. administered 75,000 IUe OMCP-OX40L for each dose, for a total of 750,000 IUe OMCP-OX40L after treatment. Group 6—The mice will be i.p. administered 75,000 IUe OMCP-OX40L mutt for each dose, for a total of 750,000 IUe OMCP-OX40L mutt after treatment. The mice will be i.p. administered 75,000 IUe OMCP-OX40L mut 2 for each dose, for a total of 750,000 IUe OMCP-OX40L mut 2 after treatment.

All tumors will be measured via caliper measurements and mouse weights measured every day during treatment. After the completion of the therapeutic course, mouse weights and tumors will be measured thrice weekly. Mice will be monitored throughout the study for signs of distress or other effects of the therapeutic treatment All mice will be euthanized at a maximum tumor diameter of 20 mm, and tumors will be reserved for later analysis. Any mice that die prematurely from known or unknown causes will have a final measurement taken and tissues collected as soon as is possible.

Potential outcomes include a finding that mice treated with OX40L may have some attenuated tumor growth and increased survival compared to saline controls. Potential outcomes further include a finding that mice treated with OX40L mut 1 or OX40L mut 2 will have little or no attenuation of tumor growth compared with the saline control mice. In comparison, potential outcomes may include a finding that treatment with OMCP-OX40L will significantly attenuate tumor growth and increase survival over both the saline, OMCP-OX40L mutt, and OMCP-OX40L mut 2 controls, as well as the OX40L group.

We will further analyze residual tumors for lymphocyte infiltration via immunohistochemistry. Specifically, we will evaluate the intratumoral infiltration of CD8+ Teff cells and NK cells. Further, we will evaluate the apoptotic levels via a TUNEL assay (Millipore ApopTag Peroxidase In Situ Apoptosis Detection Kit, Cat No. S7100). Potential outcomes include a finding that treatment with OMCP-OX40L increases CD8+ Teff an NK cell intratumoral infiltration significantly over either saline control mice or OX40L treated mice.

These results would suggest that NKG2D ligand OX40L fusion proteins, specifically OMCP-OX40L, has an increased therapeutic benefit as compared to OX40L treatment alone. Further, intratumoral infiltration of cytotoxic lymphocytes should be enhanced by the NKG2D ligand OX40L fusion protein, suggesting that targeted activation of these cellular populations increases the capacity of these cells to overcome the immunosuppression of the tumor cells.

Example 31. NKG2D Targeted Delivery of 4-1BBL Preferentially Activates Cytotoxic Lymphocytes In Vitro

This example describes in vitro testing of NKG2D targeted delivery of 4-1BBL therapies. Specifically, this example will demonstrate improved immune cell activation of OMCP-4-1BBL over purified cytokine.

A total of 4 C57131/6 mice 6-9 weeks of age will be utilized to prepare a fresh splenocyte culture. Splenocytes will be cultured in triplicate for 36 hours according to the following groups: Group 1—saline control, Group 2—100 IUe/mL 4-1BBL, Group 3—100 IUe/mL OMCP-4-1BBL. After the 36-hour culture period, cells will be stained for flow cytometry according to standard protocols, and cellular activation will be evaluated.

Cellular populations will be defined via the following gating strategies: T_regs—CD45+CD3+CD4+Foxp3+, NK cells—CD45+CD3−CD49b+CD335+, Teff—CD45+CD3+CD8+. Cellular activation will be further defined via evaluation whether the following markers are upergulated: T_regs—ICOS, NK cells—CD69 and KLRG1, Teff—CD69.

Potential outcomes include a finding that NK cells are significantly activated by treatment with 4-1BBL and OMCP-4-1BBL. Teff cells may also be activated by treatment with -1BBL and OMCP-4-1BBL. Potential outcomes further include a finding that the OMCP-4-1BBL will show greater activation of NK, and potentially Teff cells, over the 4-1BBL ligand alone.

These results would suggest that targeting 4-1BBL therapy to NKG2D expressing cells via OMCP ligand fusion protein significantly enhances the efficacy of 4-1BBL therapy in anti-tumor cell populations such as NK cells and Teff cells.

Example 32. NKG2D Targeted Delivery of 4-1BBL Induces Proliferation of Cytotoxic Lymphocytes In Vitro

This example describes in vitro testing of NKG2D targeted delivery of 4-1BBL therapies. Specifically, this example will demonstrate improved cytotoxic immune cell expansion by OMCP-4-1BBL over purified cytokine.

A total of 4 C57131/6 mice 6-9 weeks of age will be utilized to prepare a fresh splenocyte culture. Splenocytes will be stained with CFSE prior to culture. CFSE permanently binds DNA, and provides an indication of cellular proliferation via reduced fluorescence with subsequent cellular divisions. Stained splenocytes will be subsequently cultured in triplicate for 6 days according to the following groups: Group 1—saline control, Group 2—1000 IUe/mL 4-1BBL, Group 3—1000 IUe/mL OMCP-4-1BBL. After the 6-day culture period, cells will be stained for flow cytometry according to standard protocols, and cellular proliferation will be evaluated.

Cellular populations will be defined via the following gating strategies: T_regs—CD45+CD3+CD4+Foxp3+, NK cells—CD45+CD3−CD49b+CD335+, Teff—CD45+CD3+CD8+.

Potential outcomes include a finding that 4-1BBL and OMCP-4-1BBL will induce significant proliferation in the NK cell population. We may also find that Teff cells are induced to proliferate via these same treatment groups. Potential outcomes further include a finding that the NK cell to Treg cell ratio, a marker for immune cell activation and prognostic for cancer therapeutic responses, will be significantly enhanced by OMCP-4-1BBL treatment over the 4-1BBL treatment alone.

These results would suggest that targeting 4-1BBL therapy to NKG2D expressing cells via a NKG2D ligand fusion protein significantly enhances the proliferative capacity of anti-tumor cell populations such as NK cells and Teff cells.

Example 33. Lymphocyte Cytotoxicity is Enhanced by NKG2D Targeted Delivery of 4-1 BBL

This example describes in vitro testing of NKG2D targeted delivery of 4-1BBL therapies. Specifically, this example will demonstrate improved cytotoxic immune cell response after treatment with OMCP-4-1BBL over purified cytokine.

A total of 6 C57131/6 mice 6-9 weeks of age will be utilized to prepare a fresh splenocyte culture. Bulk splenocytes will be cultured for 6 days according to the following groups: Group 1—saline control, Group 2—1000 IUe/mL 4-1BBL, Group 3—1000 IUe/mL OMCP-4-1BBL. After the 6-day culture period, cells will be prepared for a 7-AAD/CFSE cytotoxicity assay against K562 cells using a kit according to the manufacturer's protocols (Cayman Chemical, 7-AAD/CFSE Cell-Mediated Cytotoxicity Assay Kit, Item No. 600120). Splenocytes from each group will be seeded with target K562 cells in triplicate at the following ratios: no target cells, 15.6:1, 31.25:1, 62.5:1, 125:1, 250:1, 500:1. After 4 hours, the live versus dead target cell ratio will be evaluated via flow cytometry.

Potential outcomes include a finding that splenocytes incubated with 4-1BBL, will have enhanced cytotoxic function against the target cells versus saline control. Potential outcomes further include a finding that OMCP-4-1BBL treatment will further enhance the cytotoxicity of the splenocytes.

These results would suggest that NKG2D ligand 4-1BBL fusion proteins increase splenocyte cytotoxic activity over 4-1BBL therapy. This may be a function of enhanced binding and signaling of the 4-1BBL portion of the fusion proteins through the 4-1BB receptor on T and NK cells.

Example 34. Tumor Growth and Survival after In Vivo Treatment with OMCP-4-1BBL Targeted Therapies

This example describes in vivo proof of concept that OMCP-4-1BBL therapies inhibit tumor or cancer progression. Specifically, this example will demonstrate improved tumor growth and overall survival metrics after in vivo treatment with OMCP-4-1 BBL fusion proteins over purified cytokine.

A total of 30 C57131/6 mice 6-9 weeks of age will be utilized. Mice will be injected with Lewis Lung Carcinoma subcutaneously at the flank with 1×105 cells per mouse. Treatment will begin 5 days later, when tumors have grown sufficiently to become visible and measurable. Initial tumor sizes and mouse weights will be taken, and mice will be randomized into groups of 10 mice such that the initial tumor sizes and mouse weights are similar between groups. The treatment groups are as follows: Group 1—saline control, Group 2—4-1BBL, Group 3—OMCP-4-1BBL.

All mice will be treated according to their groups twice daily in 12 hour intervals for 5 days, a total of 10 doses. Group 1—The mice will be intraperitoneally (i.p.) administered 200 μL saline for all treatments as a negative control. Group 2—The mice will be i.p. administered 75,000 IUe 4-1BBL for each dose, for a total of 750,000 IUe 4-1BBL after treatment. Group 3—The mice will be i.p. administered 75,000 IUe OMCP-4-1BBL for each dose, for a total of 750,000 IUe OMCP-4-1BBL after treatment.

All tumors will be measured via caliper measurements and mouse weights measured every day during treatment. After the completion of the therapeutic course, mouse weights and tumors will be measured thrice weekly. Mice will be monitored throughout the study for signs of distress or other effects of the therapeutic treatment All mice will be euthanized at a maximum tumor diameter of 20 mm, and tumors will be reserved for later analysis. Any mice that die prematurely from known or unknown causes will have a final measurement taken and tissues collected as soon as is possible.

Potential outcomes include a finding that mice treated with 4-1BBL may have some attenuated tumor growth and increased survival compared to saline controls. In comparison, Potential outcomes further include a finding that treatment with OMCP-4-1BBL will significantly attenuate tumor growth and increase survival over both the saline controls, as well as the 4-1BBL group.

We will further analyze residual tumors for lymphocyte infiltration via immunohistochemistry. Specifically, we will evaluate the intratumoral infiltration of CD8+ Teff cells and NK cells. Further, we will evaluate the apoptotic levels via a TUNEL assay (Millipore ApopTag Peroxidase In Situ Apoptosis Detection Kit, Cat No. S7100). Potential outcomes include a finding that treatment with OMCP-4-1BBL increases CD8+ Teff an NK cell intratumoral infiltration significantly over either saline control mice or 4-1BBL treated mice.

These results would suggest that NKG2D ligand 4-1BBL fusion proteins, specifically OMCP-4-1BBL, has an increased therapeutic benefit as compared to 4-1BBL treatment alone. Further, intratumoral infiltration of cytotoxic lymphocytes should be enhanced by the NKG2D ligand 4-1BBL fusion protein, suggesting that targeted activation of these cellular populations increases the capacity of these cells to overcome the immunosuppression of the tumor cells.

Example 35. OMCP-IL2 for Expanding Ex Vivo Cell Therapy Cultures

An experiment was conducted to evaluate the utility of targeted cytokine delivery on in vitro cytotoxic lymphocyte expansion. The disclosed chimeric peptides, specifically OMCP-IL2, may be used to expand T cells such as CAR-T cells or tumor infiltrating lymphocytes (TIL). These therapies are typically cultured ex vivo in the presence of IL2 to facilitate their expansion. Experiments were conducted to determine if OMCP-IL2 would expand ex vivo cultured lymphocytes better than IL2 alone.

In this study, 2.5×10⁶ C57BL/6 splenocytes were cultured in the presence of plate bound anti-CD3 and either wild-type IL-2 or OMCP-mutIL-2 at 1000 IUe/ml. The CD3 stimulation was removed after 72 hours and cytokine containing media was replenished every other day to avoid media exhaustion. The total number of CD3+ T cells and well as NK1.1⁺CD3⁻ NK cells was counted flow cytometrically over the course of 2 weeks and phenotypic markers of proliferation (KI67 expression), viability (staining by the exclusion of viability dye L34959) and exhaustion (surface PD1 expression). At the completion of the experiment (day 13) the cells were evaluated for other markers of exhaustion such as Lag3 and Tim3.

The results demonstrated that an increased number of both T and NK cells was evident in cultures expanded with OMCP-mutIL-2 over wild type IL-2 (FIG. 37 , FIG. 38 ). A similar level of proliferation was evident between the two cultures but viability of OMCP-mutIL-2 treated cells was higher, possibly explaining the increase in cell number. PD-1 levels increased in both NK and CD3+ T cells but decreased significantly by day 6-9 of culture in OMCP-mutIL-2 treated cells but not wild-type IL-2 treated cells. Other markers of exhaustion, such as Tim-2 and Lag-3 were increased in wild-type IL-2 treated cultures as well. Accordingly, these results demonstrate that OMCP-mutIL2 is more effective than wild-type IL2 at ex vivo expansion of lymphocytes. This has important implications for therapies such as adoptive cellular immunotherapies. Adoptive cellular immunotherapy is a T cell based immunotherapy whereby T cells are taken from a subject and stimulated and/or genetically manipulated in vitro and then transferred back into a patient to fight against a tumor or infection.

TABLE 5
	Atomic Coordinates for OMCP-NKG2D (4PDC).

HEADER	IMMUNE SYSTEM/VIRAL PROTEIN 17-APR-14 4PDC
TITLE	CRYSTAL STRUCTURE OF COWPOX VIRUS CPXV018 (OMCP) BOUND TO HUMAN NKG2D
COMPND	MOL_ID: 1;
COMPND	2 MOLECULE: NKG2-D TYPE II INTEGRAL MEMBRANE PROTEIN;
COMPND	3 CHAIN: A, B, C, D;
COMPND	4 FRAGMENT: UNP RESIDUES 93-215;
COMPND	5 SYNONYM: KILLER CELL LECTIN-LIKE RECEPTOR SUBFAMILY K MEMBER 1, NK
COMPND	6 CELL RECEPTOR D, NKG2-D-ACTIVATING NK RECEPTOR;
COMPND	7 ENGINEERED: YES;
COMPND	8 MOL_ID: 2;
COMPND	9 MOLECULE: CPXV018 PROTEIN;
COMPND	10 CHAIN: E, F;
COMPND	11 FRAGMENT: UNP RESIDUES 20-168;
COMPND	12 ENGINEERED: YES;
COMPND	13 MUTATION: YES
SOURCE	MOL_ID: 1;
SOURCE	2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE	4 ORGANISM_TAXID: 9606;
SOURCE	5 GENE: KLRK1, D12S2489E, NKG2D;
SOURCE	6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE	7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE	8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL;
SOURCE	9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE	10 EXPRESSION_SYSTEM_PLASMID: PET21A(+);
SOURCE	11 MOL_ID: 2;
SOURCE	12 ORGANISM_SCIENTIFIC: COWPOX VIRUS;
SOURCE	13 ORGANISM_COMMON: CPV;
SOURCE	14 ORGANISM_TAXID: 10243;
SOURCE	15 GENE: CPXV018 CDS;
SOURCE	16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE	17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE	18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL;
SOURCE	19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE	20 EXPRESSION_SYSTEM_PLASMID: PET21A(+)
KEYWDS	SECRETED VIRAL PROTEIN, IMMUNE EVASION, ORTHOPOXVIRUS, MHC-LIKE FOLD,
KEYWDS	2 NK CELL RECEPTOR LIGAND, STRUCTURAL GENOMICS, CENTER FOR STRUCTURAL
KEYWDS	3 GENOMICS OF INFECTIOUS DISEASES, CSGID, IMMUNE SYSTEM-VIRAL PROTEIN
KEYWDS	4 COMPLEX
EXPDTA	X-RAY DIFFRACTION
AUTHOR	E. LAZEAR, C. A. NELSON, D. H. FREMONT, CENTER FOR STRUCTURAL GENOMICS OF
AUTHOR	2 INFECTIOUS DISEASES (CSGID)
REVDAT	2 30-JUL-14 4PDC 1 JRNL
REVDAT	1 21-MAY-14 4PDC 0
JRNL	AUTH E. LAZEAR, M. SUN, C. A. NELSON, J. A. CAMPBELL, L. N. CARAYANNOPOULOS,
JRNL	AUTH 2 A. R. FRENCH, D. H. FREMONT,
JRNL	AUTH 3 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
JRNL	AUTH 4 (CSGID)
JRNL	TITL COWPOX VIRUS OMCP ANTAGONIZES NKG2D VIA AN UNEXPECTED
JRNL	TITL 2 BINDING ORIENTATION
JRNL	REF TO BE PUBLISHED
REMARK	2 RESOLUTION. 1.99 ANGSTROMS.
REMARK	3 REFINEMENT.
REMARK	3 PROGRAM: PHENIX (PHENIX.REFINE: 1.8.4_1496)
REMARK	3 AUTHORS: PAUL ADAMS, PAVEL AFONINE, VINCENT CHEN, IAN
REMARK
	3 REFINEMENT TARGET: ML
REMARK
	3 DATA USED IN REFINEMENT.
REMARK	3 RESOLUTION RANGE HIGH (ANGSTROMS): 1.99
REMARK	3 RESOLUTION RANGE LOW (ANGSTROMS): 45.67
REMARK	3 MIN(FOBS/SIGMA_FOBS): 1.380
REMARK	3 COMPLETENESS FOR RANGE (%): 92.9
REMARK	3 NUMBER OF REFLECTIONS: 50042
REMARK	3 FIT TO DATA USED IN REFINEMENT.
REMARK	3 R VALUE (WORKING + TEST SET): 0.168
REMARK	3 RVALUE (WORKING SET): 0.166
REMARK	3 FREE R VALUE: 0.214
REMARK	3 FREE R VALUE TEST SET SIZE (%): 3.980
REMARK	3 FREE R VALUE TEST SET COUNT: 1994
REMARK	3 FIT TO DATA USED IN REFINEMENT (IN BINS).

REMARK	3	BIN	RESOLUTION	RANGE	COMPL.	NWORK	NFREE	RWORK	RFREE
REMARK
	3	1	45.6774	−4.7969	1.00	3740	160	0.1646	0.1709
REMARK	3	2	4.7969	−3.808	1.00	3733	155	0.1289	0.1960
REMARK	3	3	3.8080	3.3268	1.00	3673	151	0.1493	0.1701
REMARK	3	4	3.3268	−3.0227	0.99	3700	158	0.1688	0.2284
REMARK	3	5	3.0227	−2.8061	0.95	3529	151	0.1864	0.2352
REMARK	3	6	2.8061	−2.6407	0.91	3353	142	0.1826	0.2189
REMARK	3	7	2.6407	−2.5084	0.90	3309	133	0.1790	0.2297
REMARK	3	8	2.5084	−2.3993	0.89	3281	134	0.1744	0.2545
REMARK	3	9	2.3993	−2.3069	0.89	3285	132	0.1778	0.2825
REMARK	3	10	2.3069	−2.2273	0.90	3327	131	0.1764	0.2197
REMARK	3	11	2.2273	−2.1577	0.90	3302	127	0.1777	0.2202
REMARK	3	12	2.1577	−2.096	0.91	3328	152	0.1834	0.2460
REMARK	3	13	2.0960	−2.0408	0.91	3341	145	0.2098	0.2812
REMARK	3	14	2.0408	−1.991	0.85	3147	123	0.2098	0.2951

REMARK	3 BULK SOLVENT MODELLING.
REMARK	3 METHOD USED: FLAT BULK SOLVENT MODEL
REMARK
	3 SOLVENT RADIUS: 1.11
REMARK	3 SHRINKAGE RADIUS: 0.90
REMARK	3 K_SOL: NULL
REMARK
	3 B_SOL: NULL
REMARK
	3 ERROR ESTIMATES.
REMARK	3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED): 0.230
REMARK	3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED): 20.990
REMARK	3 B VALUES.
REMARK	3 FROM WILSON PLOT (A**2): 21.62
REMARK	3 MEAN B VALUE (OVERALL, A**2): NULL
REMARK
	3 OVERALL ANISOTROPIC B VALUE.
REMARK	3 B11 (A**2): NULL
REMARK
	3 B22 (A**2): NULL
REMARK
	3 B33 (A**2): NULL
REMARK
	3 B12 (A**2): NULL
REMARK
	3 B13 (A**2): NULL
REMARK
	3 B23 (A**2): NULL
REMARK
	3 TWINNING INFORMATION.
REMARK	3 FRACTION: NULL
REMARK
	3 OPERATOR: NULL
REMARK
	3 DEVIATIONS FROM IDEAL VALUES.

REMARK	3		RMSD	COUNT
REMARK
	3	BOND:	0.003	6687
REMARK	3	ANGLE:	0.786	9030
REMARK	3	CHIRALITY:	0.031	933
REMARK	3	PLANARITY:	0.003	1150
REMARK	3	DIHEDRAL:	13.423	2426

REMARK	3 TLS DETAILS
REMARK	3 NUMBER OF TLS GROUPS: NULL
REMARK
	3 NCS DETAILS
REMARK
	3 NUMBER OF NCS GROUPS: NULL
REMARK
	3 OTHER REFINEMENT REMARKS: NULL
REMARK
	4 4PDC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK	100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-APR-14.
REMARK	100 THE DEPOSITION ID IS D_1000201141.
REMARK	200 EXPERIMENTAL DETAILS
REMARK	200 EXPERIMENT TYPE: X-RAY DIFFRACTION
REMARK
	200 DATE OF DATA COLLECTION: 19-OCT-10
REMARK	200 TEMPERATURE (KELVIN): 100
REMARK	200 PH: 6.75
REMARK	200 NUMBER OF CRYSTALS USED: 1
REMARK	200 SYNCHROTRON (Y/N): Y
REMARK
	200 RADIATION SOURCE: ALS
REMARK
	200 BEAMLINE: 4.2.2
REMARK	200 X-RAY GENERATOR MODEL: NULL
REMARK
	200 MONOCHROMATIC OR LAUE (M/L): M
REMARK
	200 WAVELENGTH OR RANGE (A): 1.00004
REMARK	200 MONOCHROMATOR: NULL
REMARK
	200 OPTICS: NULL
REMARK
	200 DETECTOR TYPE: CCD
REMARK
	200 DETECTOR MANUFACTURER: NOIR-1
REMARK	200 INTENSITY-INTEGRATION SOFTWARE: HKL
REMARK
	200 DATA SCALING SOFTWARE: HKL
REMARK
	200 NUMBER OF UNIQUE REFLECTIONS: 50139
REMARK	200 RESOLUTION RANGE HIGH (A): 1.991
REMARK	200 RESOLUTION RANGE LOW (A): 50.000
REMARK	200 REJECTION CRITERIA (SIGMA(I)): NULL
REMARK
	200 OVERALL.
REMARK	200 COMPLETENESS FOR RANGE (%): 93.5
REMARK	200 DATA REDUNDANCY: 6.200
REMARK	200 R MERGE (I): 0.11800
REMARK	200 R SYM (I): NULL
REMARK
	200 <I/SIGMA(I)> FOR THE DATA SET: 12.7000
REMARK	200 IN THE HIGHEST RESOLUTION SHELL.
REMARK	200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A): 2.00
REMARK	200 HIGHEST RESOLUTION SHELL, RANGE LOW (A): 2.07
REMARK	200 COMPLETENESS FOR SHELL (%): 91.5
REMARK	200 DATA REDUNDANCY IN SHELL: 5.30
REMARK	200 R MERGE FOR SHELL (I): 0.48500
REMARK	200 R SYM FOR SHELL (I): NULL
REMARK	200 <I/SIGMA(I)> FOR SHELL: NULL
REMARK	200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK	200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK	200 SOFTWARE USED: PHASER
REMARK	200 STARTING MODEL: 1MPU, 4FFE
REMARK	200 REMARK: NULL
REMARK	280 CRYSTAL
REMARK	280 SOLVENT CONTENT, VS (%): 42.94
REMARK	280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK	280 CRYSTALLIZATION CONDITIONS: 15% PEG 3350, 0.2M MGCL2, 0.1M BIS
REMARK	280 -TRIS
REMARK	290 CRYSTALLOGRAPHIC SYMMETRY
REMARK	290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK	290 SYMOP SYMMETRY
REMARK	290 NNNMMM OPERATOR
REMARK	290 1555 X,Y,Z
REMARK	290 2555 −X, Y +1/2, −Z
REMARK	290 WHERE NNN -> OPERATOR NUMBER
REMARK	290 MMM -> TRANSLATION VECTOR
REMARK	290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK	290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK	290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK	290 RELATED MOLECULES.

REMARK	290	SMYTRY1	1	1.000000	0.000000	0.000000	0.000000
REMARK	290	SMYTRY2	1	0.000000	1.000000	0.000000	0.000000
REMARK	290	SMYTRY3	1	0.000000	0.000000	1.000000	0.000000
REMARK	290	SMYTRY1	2	−1.000000	0.000000	0.000000	0.000000
REMARK	290	SMYTRY2	2	0.000000	1.000000	0.000000	50.55500
REMARK	290	SMYTRY3	2	0.000000	0.000000	−1.000000	0.000000

REMARK	290 REMARK: NULL
REMARK
	300 BIOMOLECULE: 1, 2
REMARK	300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK
	300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK	300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK	300 BURIED SURFACE AREA.
REMARK	300 REMARK: THE BIOLOGICAL UNIT OF HNKG2D IS A DIMER (CHAINS A & B AND
REMARK	300 CHAINS C & D
REMARK	350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK	350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK	350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK	350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK	350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK	350 BIOMOLECULE: 1
REMARK	350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK	350 APPLY THE FOLLOWING TO CHAINS: A, B, E

REMARK	350	BIOMT1	1.000000	1.000000	0.000000	0.000000	0.000000
REMARK	350	BIOMT2	1.000000	0.000000	1.000000	0.000000	0.000000
REMARK	350	BIOMT3	1.000000	0.000000	0.000000	1.000000	0.000000

REMARK	350 BIOMOLECULE: 2
REMARK	350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK	350 APPLY THE FOLLOWING TO CHAINS: C, D, F

REMARK	350	BIOMT1	1.000000	1.000000	0.000000	0.000000	0.000000
REMARK	350	BIOMT2	1.000000	0.000000	1.000000	0.000000	0.000000
REMARK	350	BIOMT3	1.000000	0.000000	0.000000	1.000000	0.000000

REMARK	465 MISSING RESIDUES
REMARK	465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK	465 EXPERIMENT. (M = MODEL NUMBER; RES = RESIDUE NAME; C = CHAIN
REMARK	465 IDENTIFIER; SSSEQ = SEQUENCE NUMBER; I = INSERTION CODE.)
REMARK	465 M RES C SSSEQI
REMARK	465 GLU B 93
REMARK	500 GEOMETRY AND STEREOCHEMISTRY
REMARK
	500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK
	500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.

REMARK	500	ATM1	RES C	SSEQI	ATM2	RES C	SSEQI	DISTANCE
REMARK	500	O	HOH F	293	O	HOH F	324	2.19

REMARK	500 REMARK: NULL
REMARK
	500 GEOMETRY AND STEREOCHEMISTRY
REMARK
	500 SUBTOPIC: CLOSE CONTACTS
REMARK
	500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK
	500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK	500 ANGSTROMS OF A SYMMETRY RELATEED ATOM IS ASSUMED TO BE ON A
REMARK	500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK	500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK
	500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK	500 DISTANCE CUTOFF:
REMARK	500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK
	500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS

REMARK

	500	ATM1	RES C	SSEQI	ATM2	RES C	SSEQI	SSYMOP	DISTANCE
REMARK	500	O	HOH C	301	O	HOH D	306	1655	2.15
REMARK	500	O	HOH C	318	O	HOH D	306	1655	2.19

REMARK	500 REMARK: NULL
REMARK
	500 GEOMETRY AND STEREOCHEMISTRY
REMARK
	500 SUBTOPIC: TORSION ANGLES
REMARK
	500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK	500 (M = MODEL NUMBER; RES = RESIDUE NAME; C = CHAIN IDENTIFIER;
REMARK	500 SSEQ = SEQUENCE NUMBER; I = INSERTION CODE).
REMARK	500 STANDARD TABLE:
REMARK	500 FORMAT:(10X, 13, 1X, A3, 1X, A1, 14, A1, 4X, F7.2, 3X, F7.2)
REMARK	500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI−
REMARK	500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395-1400

REMARK	500	M RES	CSSEQI	PSI	PHI
REMARK
	500	SER A	151	−170.24	71.72
REMARK	500	THR A	162	−74.87	−58.64
REMARK	500	MET A	184	−75.63	−143.50
REMARK	500	TYR B	106	114.87	−162.70
REMARK	500	SER B	151	−171.27	67.58
REMARK	500	THR B	162	−35.85	164.34
REMARK	500	MET B	184	−59.05	−140.78
REMARK	500	SER C	151	−172.20	65.21
REMARK	500	MET C	184	−64.72	−143.36
REMARK	500	SER D	151	−170.57	74.89
REMARK	500	MET D	184	−66.96	−138.40
REMARK	500	ASN E	88	16.97	57.97
REMARK	500	THR E	104	−12.21	−141.68
REMARK	500	LYS F	35	−52.70	−131.11
REMARK	500	THR F	104	−6.09	−145.54

REMARK	500 REMARK: NULL
REMARK	525 SOLVENT
REMARK	525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK	525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK	525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK	525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK	525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK	525 RES = RESIDUE NAME; C = CHAIN IDENTIFIER; SSEQ = SEQUENCE
REMARK	525 NUMBER; I = INSERTION CODE):

REMARK	525	M RES	CSSEQI
REMARK	525	HOH A	385 DISTANCE = 6.57 ANGSTROMS
REMARK	525	HOH A	387 DISTANCE = 6.32 ANGSTROMS
REMARK	525	HOH F	337 DISTANCE = 5.90 ANGSTROMS

REMARK	900 RELATED ENTRIES
REMARK	900 RELATED ID: 4FFE RELATED DB: PDB
REMARK	900 4FFE IS THE STRUCTURE OF FREE COWPOX VIRUS CPXV018 (OMCP)
REMARK	900 RELATED ID: 1MPU RELATED DB: PDB
REMARK	900 1MPU IS THE STRUCTURE OF FREE HUMAN NKG2D IMMUNORECEPTOR.
REMARK	900 RELATED ID: 1HYR RELATED DB: PDB
REMARK	900 HUMAN NKG2D IN COMPLEX WITH MIC-A
REMARK	900 RELATED ID: 1JSK RELATED DB: PDB
REMARK	900 MOUSE NKG2D IN COMPLEX WITH RAE-1BETA
REMARK	900 RELATED ID: 1KCG RELATED DB: PDB
REMARK	900 HUMAN NKG2D IN COMPLEX WITH ULBP3
REMARK	900 RELATED ID: CSGID-IDP00259 RELATED DB: TARGETTRACK

DBREF	4PDC A	93	215	UNP	P26718	NKG2D_HUMAN	93	215
DBREF	4PDC B	93	215	UNP	P26718	NKG2D_HUMAN	93	215
DBREF	4PDC C	93	215	UNP	P26718	NKG2D_HUMAN	93	215
DBREF	4PDC D	93	215	UNP	P26718	NKG2D_HUMAN	93	215
DBREF	4PDC E	1	149	UNP	Q8QN43	Q8QN43_COWPX	20	168
DBREF	4PDC F	1	149	UNP	Q8QN43	Q8QN43_COWPX	20	168

SEQADV	4PDC	GLY E	0	UNP	Q8QN43			EXPRESSION TAG
SEQADV	4PDC	ASP E	23	UNP	Q8QN43	TYR	42	ENGINEERED MUTATION
SEQADV	4PDC	ASP E	95	UNP	Q8QN43	PHE	114	ENGINEERED MUTATION
SEQADV	4PDC	GLY F	0	UNP	Q8QN43			EXPRESSION TAG
SEQADV	4PDC	ASP F	23	UNP	Q8QN43	TYR	42	ENGINEERED MUTATION
SEQADV	4PDC	ASP F	95	UNP	Q8QN43	PHE	114	ENGINEERED MUTATION

SEQRES	1 A	123	GLU SER TYR CYS GLY PRO CYS PRO LYS ASN TRP ILE CYS
SEQRES	2 A	123	TYR LYS ASN ASN CYS TYR GLN PHE PHE ASP GLU SER LYS
SEQRES	3 A	123	ASN TRP TYR GLU SER GLN ALA SER CYS MET SER GLN ASN
SEQRES	4 A	123	ALA SER LEU LEU LYS VAL TYR SER LYS GLU ASP GLN ASP
SEQRES	5 A	123	LEU LEU LYS LEU VAL LYS SER TYR HIS TRP MET GLY LEU
SEQRES	6 A	123	VAL HIS ILE PRO THR ASN GLY SER TRP GLN TRP GLU ASP
SEQRES	7 A	123	GLY SER ILE LEU SER PRO ASN LEU LEU THR ILE ILE GLU
SEQRES	8 A	123	MET GLN LYS GLY ASP CYS ALA LEU TYR ALA SER SER PHE
SEQRES	9 A	123	LYS GLY TYR ILE GLU ASN CYS SER THR PRO ASN THR TYR
SEQRES	10 A	123	ILE CYS MET GLN ARG THR
SEQRES	1 B	123	GLU SER TYR CYS GLY PRO CYS PRO LYS ASN TRP ILE CYS
SEQRES	2 B	123	TYR LYS ASN ASN CYS TYR GLN PHE PHE ASP GLU SER LYS
SEQRES	3 B	123	ASN TRP TYR GLU SER GLN ALA SER CYS MET SER GLN ASN
SEQRES	4 B	123	ALA SER LEU LEU LYS VAL TYR SER LYS GLU ASP GLN ASP
SEQRES	5 B	123	LEU LEU LYS LEU VAL LYS SER TYR HIS TRP MET GLY LEU
SEQRES	6 B	123	VAL HIS ILE PRO THR ASN GLY SER TRP GLN TRP GLU ASP
SEQRES	7 B	123	GLY SER ILE LEU SER PRO ASN LEU LEU THR ILE ILE GLU
SEQRES	8 B	123	MET GLN LYS GLY ASP CYS ALA LEU TYR ALA SER SER PHE
SEQRES	9 B	123	LYS GLY TYR ILE GLU ASN CYS SER THR PRO ASN THR TYR
SEQRES	10 B	123	ILE CYS MET GLN ARG THR
SEQRES	1 C	123	GLU SER TYR CYS GLY PRO CYS PRO LYS ASN TRP ILE CYS
SEQRES	2 C	123	TYR LYS ASN ASN CYS TYR GLN PHE PHE ASP GLU SER LYS
SEQRES	3 C	123	ASN TRP TYR GLU SER GLN ALA SER CYS MET SER GLN ASN
SEQRES	4 C	123	ALA SER LEU LEU LYS VAL TYR SER LYS GLU ASP GLN ASP
SEQRES	5 C	123	LEU LEU LYS LEU VAL LYS SER TYR HIS TRP MET GLY LEU
SEQRES	6 C	123	VAL HIS ILE PRO THR ASN GLY SER TRP GLN TRP GLU ASP
SEQRES	7 C	123	GLY SER ILE LEU SER PRO ASN LEU LEU THR ILE ILE GLU
SEQRES	8 C	123	MET GLN LYS GLY ASP CYS ALA LEU TYR ALA SER SER PHE
SEQRES	9 C	123	LYS GLY TYR ILE GLU ASN CYS SER THR PRO ASN THR TYR
SEQRES	10 C	123	ILE CYS MET GLN ARG THR
SEQRES	1 D	123	GLU SER TYR CYS GLY PRO CYS PRO LYS ASN TRP ILE CYS
SEQRES	2 D	123	TYR LYS ASN ASN CYS TYR GLN PHE PHE ASP GLU SER LYS
SEQRES	3 D	123	ASN TRP TYR GLU SER GLN ALA SER CYS MET SER GLN ASN
SEQRES	4 D	123	ALA SER LEU LEU LYS VAL TYR SER LYS GLU ASP GLN ASP
SEQRES	5 D	123	LEU LEU LYS LEU VAL LYS SER TYR HIS TRP MET GLY LEU
SEQRES	6 D	123	VAL HIS ILE PRO THR ASN GLY SER TRP GLN TRP GLU ASP
SEQRES	7 D	123	GLY SER ILE LEU SER PRO ASN LEU LEU THR ILE ILE GLU
SEQRES	8 D	123	MET GLN LYS GLY ASP CYS ALA LEU TYR ALA SER SER PHE
SEQRES	9 D	123	LYS GLY TYR ILE GLU ASN CYS SER THR PRO ASN THR TYR
SEQRES	10 D	123	ILE CYS MET GLN ARG THR
SEQRES	1 E	150	GLY HIS LYS LEU ALA PHE ASN PHE ASN LEU GLU ILE ASN
SEQRES	2 E	150	GLY SER ASP THR HIS SER THR VAL ASP VAL ASP LEU ASP
SEQRES	3 E	150	ASP SER GLN ILE ILE THR PHE ASP GLY LYS ASP ILE ARG
SEQRES	4 E	150	PRO THR ILE PRO PHE MET ILE GLY ASP GLU ILE PHE LEU
SEQRES	5 E	150	PRO PHE TYR LYS ASN VAL PHE SER GLU PHE PHE SER LEU
SEQRES	6 E	150	PHE ARG ARG VAL PRO THR SER THR PRO TYR GLU ASP LEU
SEQRES	7 E	150	THR TYR PHE TYR GLU CYS ASP TYR THR ASP ASN LYS SER
SEQRES	8 E	150	THR PHE ASP GLN ASP TYR LEU TYR ASN GLY GLU GLU TYR
SEQRES	9 E	150	THR VAL LYS THR GLN GLU ALA THR ASN LYS ASN MET TRP
SEQRES	10 E	150	LEU THR THR SER GLU PHE ARG LEU LYS LYS TRP PHE ASP
SEQRES	11 E	150	GLY GLU ASP CYS ILE MET HIS LEU ARG SER LEU VAL ARG
SEQRES	12 E	150	LYS MET GLU ASP SER LYS ARG
SEQRES	1 F	150	GLY HIS LYS LEU ALA PHE ASN PHE ASN LEU GLU ILE ASN
SEQRES	2 F	150	GLY SER ASP THR HIS SER THR VAL ASP VAL ASP LEU ASP
SEQRES	3 F	150	ASP SER GLN ILE ILE THR PHE ASP GLY LYS ASP ILE ARG
SEQRES	4 F	150	PRO THR ILE PRO PHE MET ILE GLY ASP GLU ILE PHE LEU
SEQRES	5 F	150	PRO PHE TYR LYS ASN VAL PHE SER GLU PHE PHE SER LEU
SEQRES	6 F	150	PHE ARG ARG VAL PRO THR SER THR PRO TYR GLU ASP LEU
SEQRES	7 F	150	THR TYR PHE TYR GLU CYS ASP TYR THR ASP ASN LYS SER
SEQRES	8 F	150	THR PHE ASP GLN ASP TYR LEU TYR ASN GLY GLU GLU TYR
SEQRES	9 F	150	THR VAL LYS THR GLN GLU ALA THR ASN LYS ASN MET TRP
SEQRES	10 F	150	LEU THR THR SER GLU PHE ARG LEU LYS LYS TRP PHE ASP
SEQRES	11 F	150	GLY GLU ASP CYS ILE MET HIS LEU ARG SER LEU VAL ARG
SEQRES	12 F	150	LYS MET GLU ASP SER LYS ARG

FORMUL

7 HOH *660(H2 O)

HELIX	1	AA1	ASN A	119	SER A	129	1	11
HELIX	2	AA2	GLN A	143	VAL A	149	5	7
HELIX	3	AA3	ASN B	119	SER B	129	1	11
HELIX	4	AA4	GLN B	143	VAL B	149	5	7
HELIX	5	AA5	ASN C	119	SER C	129	1	11
HELIX	6	AA6	GLN C	143	VAL C	149	5	7
HELIX	7	AA7	ASN D	119	GLN D	130	1	12
HELIX	8	AA8	GLN D	143	VAL D	149	5	7
HELIX	9	AA9	ILE E	41	ILE E	45	5	5
HELIX	10	AB1	ILE E	49	LEU E	64	1	16
HELIX	11	AB2	THR E	111	LYS E	126	1	16
HELIX	12	AB3	ASP E	129	ASP E	146	1	18
HELIX	13	AB4	ILE F	41	ILE F	45	5	5
HELIX	14	AB5	ILE F	49	LEU F	64	1	16
HELIX	15	AB6	THR F	111	LYS F	125	1	16
HELIX	16	AB7	ASP F	129	ASP F	146	1	18

Sheet1	AA1 2	SER A	94	CYS A	96 0
Sheet2	AA1 2	CYS B	96	CYS B	99−1O	CYS B	99N	SER A	94
Sheet1	AA2 4	ILE A	104	TYR A	10 6 0
Sheet2	AA2 4	ASN A	109	LYS A	11 8−1O	TYR A	111 N	ILE A	104
Sheet3	AA2 4	ASN A	207	GLN A	21 3−1O	GLN A	213 N	CYS A	110
Sheet4	AA2 4	SER A	133	LEU A	13 4−1N	SER A	133 O	MET A	212
Sheet1	AA3 4	HIS A	153	TRP A	15 4 0
Sheet2	AA3 4	CYS A	189	ALA A	19 3−1O	TYR A	192 N	HIS A	153
Sheet3	AA3 4	LYS A	197	GLU A	20 1−1O	GLU A	201 N	CYS A	189
Sheet4	AA3 4	THR A	180	ILE A	18 2 1N	ILE A	182 O	GLY A	198
Sheet1	AA4 2	LEU A	157	HIS A	15 9 0
Sheet2	AA4 2	TRP A	166	TRP A	16 8−1O	GLN A	167 N	VAL A	158
Sheet1	AA5 5	ILE B	104	TYR B	10 6 0
Sheet2	AA5 5	ASN B	109	LYS B	11 8−1O	TYR B	111 N	ILE B	104
Sheet3	AA5 5	ASN B	207	ARG B	21 4−1O	ASN B	207 N	LYS B	118
Sheet4	AA5 5	HIS B	153	HIS B	15 9 1N	TRP B	154 O	THR B	208
Sheet5	AA5 5	TRP B	166	TRP B	16 8−1O	GLN B	167 N	VAL B	158
Sheet1	AA6 6	SER B	133	LEU B	13 4 0
Sheet2	AA6 6	ASN B	207	ARG B	21 4−1O	MET B	212 N	SER B	133
Sheet3	AA6 6	HIS B	153	HIS B	15 9 1N	TRP B	154 O	THR B	208
Sheet4	AA6 6	CYS B	189	ALA B	19 3−1O	TYR B	192 N	HIS B	153
Sheet5	AA6 6	LYS B	197	GLU B	20 1−1O	LYS B	197 N	ALA B	193
Sheet6	AA6 6	THR B	180	ILE B	18 2 1N	ILE B	182 O	GLY B	198
Sheet1	AA7 2	CYS C	96	CYS C	99 0
Sheet2	AA7 2	SER D	94	CYS D	96−1O	SER D	94 N	CYS C	99
Sheet1	AA8 8	SER C	133	LEU C	13 4 0
Sheet2	AA8 8	ASN C	207	ARG C	21 4−1O	MET C	212 N	SER C	133
Sheet3	AA8 8	ASN C	109	LYS C	11 8−1N	CYS C	110 O	GLN C	213
Sheet4	AA8 8	ILE C	104	TYR C	10 6−1N	ILE C	104 O	TYR C	111
Sheet5	AA8 8	ILE D	104	TYR D	106 −1O	CYS D	105 N	CYS C	105
Sheet6	AA8 8	ASN D	109	LYS D	118 −1O	TYR D	111 N	ILE D	104
Sheet7	AA8 8	ASN D	207	GLN D	213 −1O	ASN D	207 N	LYS D	118
Sheet8	AA8 8	SER D	133	LEU D	134 −1N	SER D	133 O	MET D	212
Sheet1	AA9 5	SER C	165	TRP C	168 0
Sheet2	AA9 5	HIS C	153	ILE C	160 −1N	VAL C	158 O	GLN C	167
Sheet3	AA9 5	CYS C	189	ALA C	193 −1O	TYR C	192 N	HIS C	153
Sheet4	AA9 5	LYS C	197	GLU C	201 −1O	GLU C	201 N	CYS C	189
Sheet5	AA9 5	THR C	180	ILE C	182 1N	ILE C	182 O	GLY C	198
Sheet1	AB1 5	TRP D	166	TRP D	168 0
Sheet2	AB1 5	HIS D	153	HIS D	159 −1N	VAL D	158 O	GLN D	167
Sheet3	AB1 5	CYS D	189	ALA D	193 −1O	TYR D	192 N	HIS D	153
Sheet4	AB1 5	LYS D	197	GLU D	201 −1O	GLU D	201 N	CYS D	189
Sheet5	AB1 5	THR D	180	ILE D	182 1N	ILE D	182 O	GLY D	198
Sheet1	AB2 7	ILE E	37	PRO E	39 0
Sheet2	AB2 7	GLN E	28	PHE E	32 −1N	THR E	31 O	ARG E	38
Sheet3	AB2 7	ASP E	15	LEU E	24 −1N	VAL E	22 O	ILE E	29
Sheet4	AB2 7	HIS E	1	ASN E	12 −1N	ALA E	4 O	ASP E	23
Sheet5	AB2 7	TYR E	74	THR E	86 −1O	GLU E	75 N	ILE E	11
Sheet6	AB2 7	LYS E	89	TYR E	98 −1O	ASP E	93 N	GLU E	82
Sheet7	AB2 7	GLU E	101	TYR E	103 −1O	GLU E	101 N	TYR E	98
Sheet1	AB3 7	ILE F	37	PRO F	39 0
Sheet2	AB3 7	SER F	27	PHE F	32 −1N	THR F	31 O	ARG F	38
Sheet3	AB3 7	ASP F	15	LEU F	24 −1N	LEU F	24 O	SER F	27
Sheet4	AB3 7	HIS F	1	ASN F	12 −1N	ASN F	12 O	ASP F	15
Sheet5	AB3 7	GLU F	75	THR F	86 −1O	TYR F	81 N	PHE F	5
Sheet6	AB3 7	LYS F	89	TYR F	98 −1O	THR F	91 N	ASP F	84
Sheet7	AB3 7	GLU F	101	TYR F	103 −1O	GLU F	101 N	TYR F	98

SSBOND	1	CYS A	96	CYS A	105	1555	1555	2.05
SSBOND	2	CYS A	99	CYS A	110	1555	1555	2.03
SSBOND	3	CYS A	127	CYS A	211	1555	1555	2.04
SSBOND	4	CYS A	189	CYS A	203	1555	1555	2.03
SSBOND	5	CYS B	96	CYS B	105	1555	1555	2.03
SSBOND	6	CYS B	99	CYS B	110	1555	1555	2.03
SSBOND	7	CYS B	127	CYS B	211	1555	1555	2.04
SSBOND	8	CYS B	189	CYS B	203	1555	1555	2.04
SSBOND	9	CYS C	96	CYS C	105	1555	1555	2.03
SSBOND	10	CYS C	99	CYS C	110	1555	1555	2.03
SSBOND	11	CYS C	127	CYS C	211	1555	1555	2.03
SSBOND	12	CYS C	189	CYS C	203	1555	1555	2.04
SSBOND	13	CYS D	96	CYS D	105	1555	1555	2.04
SSBOND	14	CYS D	99	CYS D	110	1555	1555	2.03
SSBOND	15	CYS D	127	CYS D	211	1555	1555	2.04
SSBOND	16	CYS D	189	CYS D	203	1555	1555	2.04
SSBOND	17	CYS E	83	CYS E	133	1555	1555	2.06
SSBOND	18	CYS F	83	CYS F	133	1555	1555	2.06

CISPEP 1	GLY A	97	PRO A	98	0	1.2
CISPEP 2	SER A	194	SER A	195	0	−3.36
CISPEP 3	GLY B	97	PRO B	98	0	1.05
CISPEP 4	SER B	194	SER B	195	0	−1.59
CISPEP 5	GLY C	97	PRO C	98	0	2.4
CISPEP 6	SER C	194	SER C	195	0	1.38
CISPEP 7	GLY D	97	PRO D	98	0	0.65
CISPEP 8	SER D	194	SER D	195	0	−3.12

CRYST1    43.315     101.11     91.368    90    91.63   90 P    1    21       8

ORIGX1	1.000000	0.000000	0.000000	0.00000
ORIGX2	0.000000	1.000000	0.000000	0.00000
ORIGX3	0.000000	0.000000	1.000000	0.00000
SCALE1	0.023087	0.000000	0.000659	0.00000
SCALE2	0.000000	0.009890	0.000000	0.00000
SCALE3	0.000000	0.000000	0.010949	0.00000

ATOM	1	N	GLU A	93	−14.924	7.066	−22.137	1	59.38	N
ATOM	2	CA	GLU A	93	−14.415	6.924	−23.496	1	58.81	C
ATOM	3	C	GLU A	93	−15.44	6.231	−24.389	1	56.95	C
ATOM	4	O	GLU A	93	−16.124	5.303	−23.956	1	61.11	O
ATOM	5	CB	GLU A	93	−13.098	6.143	−23.497	1	60	C
ATOM	6	CG	GLU A	93	−13.22	4.711	−22.996	1	72.71	C
ATOM	7	CD	GLU A	93	−11.88	3.998	−22.928	1	80.57	C
ATOM	8	OE1	GLU A	93	−10.846	4.64	−23.211	1	79.10	O
ATOM	9	OE2	GLU A	93	−11.862	2.794	−22.593	1	85.72	O1−
ATOM	10	HA	GLU A	93	−14.242	7.805	−23.864	1	70.57	H
ATOM	11	HB2	GLU A	93	−12.756	6.11	−24.404	1	72	H
ATOM	12	HB3	GLU A	93	−12.464	6.603	−22.925	1	72	H
ATOM	13	HG2	GLU A	93	−13.601	4.719	−22.104	1	87.25	H
ATOM	14	HG3	GLU A	93	−13.794	4.213	−23.598	1	87.25	H
ATOM	15	N	SER A	94	−15.537	6.687	−25.634	1	47.51	N
ATOM	16	CA	SER A	94	−16.522	6.163	−26.571	1	43.6	C
ATOM	17	C	SER A	94	−15.911	5.889	−27.937	1	40.17	C
ATOM	18	O	SER A	94	−14.793	6.312	−28.231	1	42.4	O
ATOM	19	CB	SER A	94	−17.684	7.143	−26.716	1	50.65	C
ATOM	20	OG	SER A	94	−17.227	8.391	−27.207	1	53.61	O
ATOM	21	H	SER A	94	−15.038	7.306	−25.963	1	57.02	H
ATOM	22	HA	SER A	94	−16.874	5.328	−26.226	1	52.32	H
ATOM	23	HB2	SER A	94	−18.332	6.777	−27.339	1	60.78	H
ATOM	24	HB3	SER A	94	−18.096	7.276	−25.848	1	60.78	H
ATOM	25	HG	SER A	94	−17.873	8.923	−27.284	1	64.33	H
ATOM	26	N	TYR A	95	−16.662	5.174	−28.766	1	37.41	N
ATOM	27	CA	TYR A	95	−16.245	4.875	−30.126	1	36.16	C
ATOM	28	C	TYR A	95	−16.815	5.907	−31.089	1	32.15	C
ATOM	29	O	TYR A	95	−17.812	6.566	−30.789	1	28.55	O
ATOM	30	CB	TYR A	95	−16.696	3.473	−30.528	1	35.46	C
ATOM	31	CG	TYR A	95	−15.877	2.361	−29.913	1	39.96	C
ATOM	32	CD1	TYR A	95	−16.234	1.797	−28.694	1	39.91	C
ATOM	33	CD2	TYR A	95	−14.75	1.87	−30.557	1	39.04	C
ATOM	34	CE1	TYR A	95	−15.488	0.775	−28.135	1	45.29	C
ATOM	35	CE2	TYR A	95	−13.998	0.85	−30.006	1	44.91	C
ATOM	36	CZ	TYR A	95	−14.37	0.306	−28.795	1	46.64	C
ATOM	37	OH	TYR A	95	−13.617	−0.71	−28.249	1	43.67	O
ATOM	38	H	TYR A	95	−17.43	4.846	−28.559	1	44.89	H
ATOM	39	HA	TYR A	95	−15.278	4.91	−30.179	1	43.39	H
ATOM	40	HB2	TYR A	95	−17.617	3.35	−30.25	1	42.56	H
ATOM	41	HB3	TYR A	95	−16.63	3.389	−31.492	1	42.56	H
ATOM	42	HD1	TYR A	95	−16.988	2.111	−28.248	1	46.85	H
ATOM	43	HD2	TYR A	95	−14.496	2.234	−31.374	1	47.89	H
ATOM	44	HE1	TYR A	95	−15.737	0.407	−27.318	1	54.35	H
ATOM	45	HE2	TYR A	95	−13.244	0.533	−30.449	1	53.9	H
ATOM	46	HH	TYR A	95	−13.948	−0.951	−27.516	1	52.4	H
ATOM	47	N	CYS A	96	−16.167	6.043	−32.241	1	28.25	N
ATOM	48	CA	CYS A	96	−16.597	6.969	−33.278	1	23.26	C
ATOM	49	C	CYS A	96	−16.818	6.214	−34.584	1	27.35	C
ATOM	50	O	CYS A	96	−15.989	5.397	−34.985	1	25.95	O
ATOM	51	CB	CYS A	96	−15.561	8.079	−33.472	1	25.56	C
ATOM	52	SG	CYS A	96	−16.018	9.334	−34.695	1	27.03	S
ATOM	53	H	CYS A	96	−15.46	5.599	−32.448	1	33.9	H
ATOM	54	HA	CYS A	96	−17.437	7.378	−33.016	1	27.92	H
ATOM	55	HB2	CYS A	96	−15.428	8.53	−32.624	1	30.68	H
ATOM	56	HB3	CYS A	96	−14.727	7.677	−33.761	1	30.68	H
ATOM	57	N	GLY A	97	−17.937	6.497	−35.244	1	24.78	N
ATOM	58	CA	GLY A	97	−18.277	5.84	−36.491	1	28.73	C
ATOM	59	C	GLY A	97	−19.711	5.345	−36.494	1	30.42	C
ATOM	60	O	GLY A	97	−20.56	5.912	−35.807	1	28.09	O
ATOM	61	H	GLY A	97	−18.52	7.074	−34.984	1	29.73	H
ATOM	62	HA2	GLY A	97	−18.162	6.46	−37.228	1	34.47	H
ATOM	63	HA3	GLY A	97	−17.688	5.082	−36.63	1	34.47	H
ATOM	64	N	PRO A	98	−19.994	4.281	−37.266	1	30.69	N
ATOM	65	CA	PRO A	98	−19.033	3.536	−38.091	1	29.74	C
ATOM	66	C	PRO A	98	−18.509	4.341	−39.28	1	26.22	C
ATOM	67	O	PRO A	98	−19.241	5.13	−39.878	1	28.36	O
ATOM	68	CB	PRO A	98	−19.843	2.324	−38.566	1	27.73	C
ATOM	69	CG	PRO A	98	−21.247	2.772	−38.528	1	29.99	C
ATOM	70	CD	PRO A	98	−21.353	3.723	−37.371	1	26.89	C
ATOM	71	HA	PRO A	98	−18.286	3.234	−37.551	1	35.69	H
ATOM	72	HB2	PRO A	98	−19.581	2.088	−39.469	1	33.28	H
ATOM	73	HB3	PRO A	98	−19.703	1.579	−37.96	1	33.28	H
ATOM	74	HG2	PRO A	98	−21.466	3.222	−39.358	1	35.98	H
ATOM	75	HG3	PRO A	98	−21.827	2.006	−38.392	1	35.98	H
ATOM	76	HD2	PRO A	98	−21.993	4.424	−37.567	1	32.27	H
ATOM	77	HD3	PRO A	98	−21.585	3.244	−36.559	1	32.27	H
ATOM	78	N	CYS A	99	−17.232	4.142	−39.591	1	22.72	N
ATOM	79	CA	CYS A	99	−16.582	4.768	−40.737	1	27.89	C
ATOM	80	C	CYS A	99	−15.575	3.793	−41.326	1	21.11	C
ATOM	81	O	CYS A	99	−15.165	2.848	−40.653	1	25.21	O
ATOM	82	CB	CYS A	99	−15.865	6.062	−40.337	1	25.67	C
ATOM	83	SG	CYS A	99	−16.919	7.351	−39.649	1	24.92	S
ATOM	84	H	CYS A	99	−16.707	3.634	−39.138	1	27.26	H
ATOM	85	HA	CYS A	99	−17.245	4.977	−41.414	1	33.47	H
ATOM	86	HB2	CYS A	99	−15.194	5.847	−39.67	1	30.81	H
ATOM	87	HB3	CYS A	99	−15.433	6.429	−41.124	1	30.81	H
ATOM	88	N	PRO A	100	−15.165	4.018	−42.583	1	24.66	N
ATOM	89	CA	PRO A	100	−14.053	3.244	−43.146	1	24.78	C
ATOM	90	C	PRO A	100	−12.777	3.4	−42.312	1	27.64	C
ATOM	91	O	PRO A	100	−12.552	4.46	−41.723	1	21.92	O
ATOM	92	CB	PRO A	100	−13.882	3.841	−44.546	1	25.09	C
ATOM	93	CG	PRO A	100	−15.217	4.427	−44.874	1	26.97	C
ATOM	94	CD	PRO A	100	−15.757	4.935	−43.574	1	24.88	C
ATOM	95	HA	PRO A	100	−14.288	2.306	−43.216	1	29.73	H
ATOM	96	HB2	PRO A	100	−13.199	4.53	−44.527	1	30.11	H
ATOM	97	HB3	PRO A	100	−13.649	3.141	−45.175	1	30.11	H
ATOM	98	HG2	PRO A	100	−15.108	5.153	−45.507	1	32.37	H
ATOM	99	HG3	PRO A	100	−15.795	3.738	−45.239	1	32.37	H
ATOM	100	HD2	PRO A	100	−15.458	5.844	−43.415	1	29.86	H
ATOM	101	HD3	PRO A	100	−16.725	4.87	−43.56	1	29.86	H
ATOM	102	N	LYS A	101	−11.958	2.356	−42.268	1	25.51	N
ATOM	103	CA	LYS A	101	−10.803	2.317	−41.372	1	31.26	C
ATOM	104	C	LYS A	101	−9.762	3.391	−41.68	1	29.73	C
ATOM	105	O	LYS A	101	−9.072	3.864	−40.778	1	35.56	O
ATOM	106	CB	LYS A	101	−10.142	0.936	−41.429	1	34.82	C
ATOM	107	CG	LYS A	101	−10.941	−0.169	−40.743	1	42.12	C
ATOM	108	CD	LYS A	101	−10.935	−0.038	−39.222	1	53.27	C
ATOM	109	CE	LYS A	101	−9.57	−0.367	−38.628	1	64.08	C
ATOM	110	NZ	LYS A	101	−9.569	−0.299	−37.138	1	67.45	+
ATOM	111	H	LYS A	101	−12.048	1.65	−42.75	1	30.62	H
ATOM	112	HA	LYS A	101	−11.111	2.46	−40.464	1	37.51	H
ATOM	113	HB2	LYS A	101	−10.027	0.684	−42.358	1	41.79	H
ATOM	114	HB3	LYS A	101	−9.276	0.988	−40.994	1	41.79	H
ATOM	115	HG2	LYS A	101	−11.862	−0.127	−41.045	1	50.54	H
ATOM	116	HG3	LYS A	101	−10.554	−1.028	−40.973	1	50.54	H
ATOM	117	HD2	LYS A	101	−11.158	0.874	−38.979	1	63.92	H
ATOM	118	HD3	LYS A	101	−11.585	−0.652	−38.846	1	63.92	H
ATOM	119	HE2	LYS A	101	−9.319	−1.267	−38.889	1	76.89	H
ATOM	120	HE3	LYS A	101	−8.917	0.27	−38.959	1	76.89	H
ATOM	121	HZ1	LYS A	101	−8.759	−0.496	−36.825	1	80.94	H
ATOM	122	HZ2	LYS A	101	−9.791	0.52	−36.87	1	80.94	H
ATOM	123	HZ3	LYS A	101	−10.156	−0.88	−36.807	1	80.94	H
ATOM	124	N	ASN A	102	−9.648	3.77	−42.949	1	25.43	N
ATOM	125	CA	ASN A	102	−8.65	4.749	−43.37	1	29.54	C
ATOM	126	C	ASN A	102	−9.227	6.159	−43.532	1	27.18	C
ATOM	127	O	ASN A	102	−8.621	7.013	−44.18	1	24.09	O
ATOM	128	CB	ASN A	102	−7.995	4.294	−44.68	1	34.94	C
ATOM	129	CG	ASN A	102	−9.006	3.828	−45.715	1	30.75	C
ATOM	130	OD1	ASN A	102	−10.215	3.951	−45.52	1	34.9	O
ATOM	131	ND2	ASN A	102	−8.512	3.285	−46.823	1	37.11	N
ATOM	132	H	ASN A	102	−10.139	3.473	−43.589	1	30.52	H
ATOM	133	HA	ASN A	102	−7.956	4.793	−42.695	1	35.45	H
ATOM	134	HB2	ASN A	102	−7.498	5.035	−45.06	1	41.92	H
ATOM	135	HB3	ASN A	102	−7.396	3.554	−44.493	1	41.92	H
ATOM	136	HD21	ASN A	102	−9.043	3.006	−47.439	1	44.53	H
ATOM	137	HD22	ASN A	102	−7.661	3.213	−46.923	1	44.53	H
ATOM	138	N	TRP A	103	−10.392	6.399	−42.932	1	22.81	N
ATOM	139	CA	TRP A	103	−11.038	7.712	−42.979	1	22.94	C
ATOM	140	C	TRP A	103	−11.012	8.411	−41.623	1	21.34	C
ATOM	141	O	TRP A	103	−10.915	7.764	−40.583	1	18.27	O
ATOM	142	CB	TRP A	103	−12.492	7.586	−43.443	1	21.32	C
ATOM	143	CG	TRP A	103	−12.658	7.417	−44.919	1	26.61	C
ATOM	144	CD1	TRP A	103	−11.883	6.664	−45.755	1	30.04	C
ATOM	145	CD2	TRP A	103	−13.663	8.023	−45.738	1	23.17	C
ATOM	146	NE1	TRP A	103	−12.351	6.759	−47.044	1	29.11	N
ATOM	147	CE2	TRP A	103	−13.442	7.588	−47.061	1	26.93	C
ATOM	148	CE3	TRP A	103	−14.731	8.887	−45.481	1	20.7	C
ATOM	149	CZ2	ARP A	103	−14.249	7.99	−48.123	1	28.53	C
ATOM	150	CZ3	TRP A	103	−15.53	9.286	−46.534	1	24.02	C
ATOM	151	CH2	TRP A	103	−15.285	8.837	−47.841	1	22.8	C
ATOM	152	H	TRP A	103	−10.834	5.812	−42.486	1	27.37	H
ATOM	153	HA	TRP A	103	−10.568	8.273	−43.616	1	27.52	H
ATOM	154	HB2	TRP A	103	−12.889	6.814	−43.011	1	25.59	H
ATOM	155	HB3	TRP A	103	−12.971	8.389	−43.183	1	25.59	H
ATOM	156	HD1	TRP A	103	−11.15	6.157	−45.49	1	36.05	H
ATOM	157	HE1	TRP A	103	−12.012	6.365	−47.729	1	34.93	H
ATOM	158	HE3	TRP A	103	−14.9	9.188	−44.618	1	24.84	H
ATOM	159	HZ2	TRP A	103	−14.088	7.695	−48.99	1	34.23	H
ATOM	160	HZ3	TRP A	103	−16.243	9.861	−46.374	1	28.82	H
ATOM	161	HH2	TRP A	103	−15.84	9.122	−48.531	1	27.37	H
ATOM	162	N	ILE A	104	−11.122	9.737	−41.653	1	15.59	N
ATOM	163	CA	ILE A	104	−11.21	10.546	−40.444	1	17.76	C
ATOM	164	C	ILE A	104	−12.621	10.491	−39.868	1	21.68	C
ATOM	165	O	ILE A	104	−13.587	10.764	−40.577	1	20.98	O
ATOM	166	CB	ILE A	104	−10.853	12.022	−40.718	1	19.18	C
ATOM	167	CG1	ILE A	104	−9.47	12.139	−41.368	1	22.53	C
ATOM	168	CG2	ILE A	104	−10.91	12.835	−39.425	1	20.64	C
ATOM	169	CD1	ILE A	104	−9.156	13.53	−41.903	1	18.1	C
ATOM	170	H	ILE A	104	−11.147	10.199	−42.378	1	18.71	H
ATOM	171	HA	ILE A	104	−10.594	10.201	−39.779	1	21.31	H
ATOM	172	HB	ILE A	104	−11.51	12.384	−41.333	1	23.02	H
ATOM	173	HG12	ILE A	104	−8.795	11.917	−40.708	1	27.03	H
ATOM	174	HG13	ILE A	104	−9.421	11.518	−42.111	1	27.03	H
ATOM	175	HG21	ILE A	104	−10.683	13.757	−39.622	1	24.77	H
ATOM	176	HG22	ILE A	104	−11.808	12.785	−39.061	1	24.77	H
ATOM	177	HG23	ILE A	104	−10.275	12.465	−38.792	1	24.77	H
ATOM	178	HD11	ILE A	104	−8.27	13.523	−42.297	1	21.72	H
ATOM	179	HD12	ILE A	104	−9.815	13.765	−42.575	1	21.72	H
ATOM	180	HD13	ILE A	104	−9.189	14.164	−41.171	1	21.72	H
ATOM	181	N	CYS A	105	−12.734	10.151	−38.587	1	19.34	N
ATOM	182	CA	CYS A	105	−14.026	10.133	−37.909	1	18.07	C
ATOM	183	C	CYS A	105	−14.117	11.285	−36.914	1	21.22	C
ATOM	184	O	CYS A	105	−13.216	11.497	−36.102	1	21.2	O
ATOM	185	CB	CYS A	105	−14.249	8.8	−37.196	1	23.12	C
ATOM	186	SG	CYS A	105	−15.944	8.565	−36.591	1	26.35	S
ATOM	187	H	CYS A	105	−12.073	9.926	−38.085	1	23.2	H
ATOM	188	HA	CYS A	105	−14.731	10.246	−38.566	1	21.68	H
ATOM	189	HB2	CYS A	105	−14.053	8.079	−37.814	1	27.74	H
ATOM	190	HB3	CYS A	105	−13.653	8.75	−36.433	1	27.74	H
ATOM	191	N	TYR A	106	−15.207	12.035	−37	1	17.94	N
ATOM	192	CA	TYR A	106	−15.451	13.148	−36.097	1	18.87	C
ATOM	193	C	TYR A	106	−16.943	13.284	−35.857	1	20.09	C
ATOM	194	O	TYR A	106	−17.711	13.548	−36.785	1	17.41	O
ATOM	195	CB	TYR A	106	−14.881	14.452	−36.659	1	17.9	C
ATOM	196	CG	TYR A	106	−14.966	15.613	−35.696	1	17.46	C
ATOM	197	CD1	TYR A	106	−14.351	15.552	−34.452	1	24.97	C
ATOM	198	CD2	TYR A	106	−15.651	16.774	−36.031	1	21.85	C
ATOM	199	CE1	TYR A	106	−14.424	16.61	−33.562	1	22.33	C
ATOM	200	CE2	TYR A	106	−15.726	17.841	−35.148	1	20.74	C
ATOM	201	CZ	TYR A	106	−15.112	17.752	−33.915	1	22.72	C
ATOM	202	OH	TYR A	106	−15.177	18.806	−33.03	1	19.96	O
ATOM	203	H	TYR A	106	−15.829	11.918	−37.582	1	21.53	H
ATOM	204	HA	TYR A	106	−15.021	12.971	35.245	1	22.65	H
ATOM	205	HB2	TYR A	106	−13.947	14.316	−36.88	1	21.49	H
ATOM	206	HB3	TYR A	106	−15.377	14.692	−37.458	1	21.49	H
ATOM	207	HD1	TYR A	106	−13.888	14.783	−34.209	1	29.97	H
ATOM	208	HD2	TYR A	106	−16.068	16.836	−36.86	1	26.22	H
ATOM	209	HE1	TYR A	106	−14.008	16.553	−32.732	1	26.79	H
ATOM	210	HE2	TYR A	106	−16.19	18.611	−35.385	1	24.89	H
ATOM	211	HH	TYR A	106	−15.622	19.435	−33.364	1	23.95	H
ATOM	212	N	LYS A	107	−17.336	13.091	−34.602	1	16.9	N
ATOM	213	CA	LYS A	107	−18.732	13.154	−34.19	1	20.74	C
ATOM	214	C	LYS A	107	−19.605	12.235	−35.048	1	17.68	C
ATOM	215	O	LYS A	107	−20.703	12.597	−35.458	1	16.31	O
ATOM	216	CB	LYS A	107	−19.221	14.602	−34.239	1	23.06	C
ATOM	217	CG	LYS A	107	−18.453	15.502	−33.268	1	17.83	C
ATOM	218	CD	LYS A	107	−18.965	16.932	−33.266	1	24.69	C
ATOM	219	CE	LYS A	107	−18.353	17.73	−32.122	1	26.16	C
ATOM	220	NZ	LYS A	107	−18.797	19.153	−32.118	1	29.75	N1+
ATOM	221	H	LYS A	107	−16.797	12.917	−33.955	1	20.28	H
ATOM	222	HA	LYS A	107	−18.8	12.851	−33.271	1	24.89	H
ATOM	223	HB2	LYS A	107	−19.096	14.949	−35.136	1	27.68	H
ATOM	224	HB3	LYS A	107	−20.16	14.629	−33.998	1	27.68	H
ATOM	225	HG2	LYS A	107	−18.545	15.149	−32.369	1	21.4	H
ATOM	226	HG3	LYS A	107	−17.518	15.519	−33.524	1	21.4	H
ATOM	227	HD2	LYS A	107	−18.723	17.362	−34.102	1	29.63	H
ATOM	228	HD3	LYS A	107	−19.929	16.929	−33.155	1	29.63	H
ATOM	229	HE2	LYS A	107	−18.618	17.329	−31.279	1	31.4	H
ATOM	230	HE3	LYS A	107	−17.387	17.716	−32.208	1	31.4	H
ATOM	231	HZ1	LYS A	107	−18.421	19.587	−31.438	1	35.7	H
ATOM	232	HZ2	LYS A	107	−18.56	19.548	−32.88	1	35.7	H
ATOM	233	HZ3	LYS A	107	−19.682	19.195	−32.034	1	35.7	H
ATOM	234	N	ASN A	108	−19.079	11.04	−35.303	1	22.6	N
ATOM	235	CA	ASN A	108	−19.77	9.979	−36.04	1	25.82	C
ATOM	236	C	ASN A	108	−20.056	10.31	−37.506	1	27.7	C
ATOM	237	O	ASN A	108	−20.822	9.609	−38.164	1	25.85	O
ATOM	238	CB	ASN A	108	−21.069	9.606	−35.324	1	25.22	C
ATOM	239	CG	ASN A	108	−20.816	8.947	−33.984	1	29.09	C
ATOM	240	OD1	ASN A	108	−19.803	8.274	−33.796	1	25.84	O
ATOM	241	ND2	ASN A	108	−21.733	9.139	−33.043	1	32.94	N
ATOM	242	H	ASN A	108	−18.29	10.81	−35.05	1	27.12	H
ATOM	243	HA	ASN A	108	−19.204	9.191	−36.033	1	30.98	H
ATOM	244	HB2	ASN A	108	−21.59	10.41	−35.172	1	30.27	H
ATOM	245	HB3	ASN A	108	−21.569	8.984	−35.876	1	30.27	H
ATOM	246	HD21	ASN A	108	−21.632	8.784	−32.266	1	39.52	H
ATOM	247	HD22	ASN A	108	−22.427	9.617	−33.21	1	39.52	H
ATOM	248	N	ASN A	109	−19.429	11.369	−38.013	1	18.88	N
ATOM	249	CA	ASN A	109	−19.347	11.605	−39.45	1	16.87	C
ATOM	250	C	ASN A	109	−17.968	11.166	−39.936	1	20.87	C
ATOM	251	O	ASN A	109	−17.001	11.227	−39.174	1	18.96	O
ATOM	252	CB	ASN A	109	−19.587	13.078	−39.786	1	18.38	C
ATOM	253	CG	ASN A	109	−21.004	13.525	−39.487	1	25.45	C
ATOM	254	OD1	ASN A	109	−21.96	12.779	−39.697	1	23.05	O
ATOM	255	ND2	ASN A	109	−21.145	14.749	−38.994	1	21.26	N
ATOM	256	H	ASN A	109	−19.038	11.971	−37.539	1	22.66	H
ATOM	257	HA	ASN A	109	−20.019	11.072	−39.905	1	20.25	H
ATOM	258	HB2	ASN A	109	−18.983	13.625	−39.259	1	22.05	H
ATOM	259	HB3	ASN A	109	−19.422	13.218	−40.731	1	22.05	H
ATOM	260	HD21	ASN A	109	−21.929	15.05	−38.808	1	25.51	H
ATOM	261	HD22	ASN A	109	−20.453	15.242	−38.862	1	25.51	H
ATOM	262	N	CYS A	110	−17.878	10.721	−41.188	1	16.93	N
ATOM	263	CA	CYS A	110	−16.608	10.264	−41.76	1	16.78	C
ATOM	264	C	CYS A	110	−16.142	11.205	−42.866	1	19.88	C
ATOM	265	O	CYS A	110	−16.951	11.666	−43.665	1	18.76	O
ATOM	266	CB	CYS A	110	−16.748	8.846	−42.312	1	23.56	C
ATOM	267	SG	CYS A	110	−17.888	7.805	−41.378	1	24.98	S
ATOM	268	H	CYS A	110	−18.543	10.673	−41.732	1	20.32	H
ATOM	269	HA	CYS A	110	−15.931	10.253	−41.065	1	20.14	H
ATOM	270	HB2	CYS A	110	−17.074	8.898	−43.224	1	28.27	H
ATOM	271	HB3	CYS A	110	−15.878	8.419	−42.297	1	28.27	H
ATOM	272	N	TYR A	111	−14.842	11.489	−42.904	1	14.28	N
ATOM	273	CA	TYR A	111	−14.262	12.364	−43.921	1	17.86	C
ATOM	274	C	TYR A	111	−12.987	11.787	−44.505	1	17.19	C
ATOM	275	O	TYR A	111	−12.298	10.99	−43.866	1	20.29	O
ATOM	276	CB	TYR A	111	−13.932	13.74	−43.342	1	15.15	C
ATOM	277	CG	TYR A	111	−15.08	14.434	−42.669	1	16.62	C
ATOM	278	CD1	TYR A	111	−15.332	14.246	−41.317	1	16.48	C
ATOM	279	CD2	TYR A	111	−15.907	15.292	−43.381	1	18.87	C
ATOM	280	CE1	TYR A	111	−16.382	14.887	−40.694	1	16.82	C
ATOM	281	CE2	TYR A	111	−16.956	15.935	−42.77	1	19.83	C
ATOM	282	CZ	TYR A	111	−17.191	15.73	−41.425	1	18.41	C
ATOM	283	OH	TYR A	111	−18.242	16.373	−40.816	1	19.61	O
ATOM	284	H	TYR A	111	−14.266	11.182	−42.343	1	17.13	H
ATOM	285	HA	TYR A	111	−14.901	12.482	−44.642	1	21.43	H
ATOM	286	HB2	TYR A	111	−13.226	13.638	−42.685	1	18.18	H
ATOM	287	HB3	TYR A	111	−13.625	14.313	−44.063	1	18.18	H
ATOM	288	HD1	TYR A	111	−14.786	13.677	−40.825	1	19.77	H
ATOM	289	HD2	TYR A	111	−15.751	15.431	−44.287	1	22.65	H
ATOM	290	HE1	TYR A	111	−16.543	14.75	−39.788	1	20.19	H
ATOM	291	HE2	TYR A	111	−17.505	16.505	−43.259	1	23.79	H
ATOM	292	HH	TYR A	111	−18.275	16.163	−40.004	1	23.53	H
ATOM	293	N	GLN A	112	−12.659	12.214	−45.716	1	18.48	N
ATOM	294	CA	GLN A	112	−11.331	11.972	−46.254	1	20.7	C
ATOM	295	C	GLN A	112	−10.973	13.053	−47.256	1	20.13	C
ATOM	296	O	GLN A	112	−11.806	13.479	−48.055	1	20.24	O
ATOM	297	CB	GLN A	112	−11.233	10.591	−46.905	1	24.04	C
ATOM	298	CG	GLN A	112	−9.818	10.232	−47.369	1	23.23	C
ATOM	299	CD	GLN A	112	−8.771	10.4	−46.272	1	29.49	C
ATOM	300	OE1	GLN A	112	−8.311	11.511	−45.994	1	31.23	O
ATOM	301	NE2	GLN A	112	−8.392	9.296	−45.645	1	30.5	N
ATOM	302	H	GLN A	112	−13.184	12.644	−46.244	1	22.17	H
ATOM	303	HA	GLN A	112	−10.687	12.008	−45.53	1	24.84	H
ATOM	304	HB2	GLN A	112	−11.513	9.921	−46.262	1	28.85	H
ATOM	305	HB3	GLN A	112	−11.815	10.567	−47.68	1	28.85	H
ATOM	306	HG2	GLN A	112	−9.806	9.306	−47.655	1	27.88	H
ATOM	307	HG3	GLN A	112	−9.573	10.811	−48.108	1	27.88	H
ATOM	308	HE21	GLN A	112	−7.804	9.338	−45.018	1	36.6	H
ATOM	309	HE22	GLN A	112	−8.733	8.538	−45.864	1	36.6	H
ATOM	310	N	PHE A	113	−9.722	13.492	−47.189	1	18.31	N
ATOM	311	CA	PHE A	113	−9.211	14.536	−48.062	1	22.45	C
ATOM	312	C	PHE A	113	−8.399	13.908	−49.187	1	18.61	C
ATOM	313	O	PHE A	113	−7.556	13.051	−48.936	1	23.89	O
ATOM	314	CB	PHE A	113	−8.36	15.523	−47.259	1	23.17	C
ATOM	315	CG	PHE A	113	−9.135	16.272	−46.211	1	24.24	C
ATOM	316	CD1	PHE A	113	−9.569	15.633	−45.06	1	29.05	C
ATOM	317	CD2	PHE A	113	−9.431	17.615	−46.375	1	27.58	C
ATOM	318	CE1	PHE A	113	−10.287	16.317	−44.096	1	26.86	C
ATOM	319	CE2	PHE A	113	−10.149	18.306	−45.412	1	28.41	C
ATOM	320	CZ	PHE A	113	−10.574	17.655	−44.272	1	30.18	C
ATOM	321	H	PHE A	113	−9.138	13.192	−46.634	1	21.97	H
ATOM	322	HA	PHE A	113	−9.954	15.021	−48.454	1	26.94	H
ATOM	323	HB2	PHE A	113	−7.651	15.034	−46.812	1	27.81	H
ATOM	324	HB3	PHE A	113	−7.977	16.174	−47.868	1	27.81	H
ATOM	325	HD1	PHE A	113	−9.379	14.731	−44.936	1	34.86	H
ATOM	326	HD2	PHE A	113	−9.147	18.058	−47.142	1	33.09	H
ATOM	327	HE1	PHE A	113	−10.572	15.877	−43.328	1	32.23	H
ATOM	328	HE2	PHE A	113	−10.342	19.208	−45.533	1	34.1	H
ATOM	329	HZ	PHE A	113	−11.055	18.118	−43.624	1	36.22	H
ATOM	330	N	PHE A	114	−8.669	14.324	−50.42	1	16.59	N
ATOM	331	CA	PHE A	114	−7.977	13.782	−51.589	1	20.44	C
ATOM	332	C	PHE A	114	−7.12	14.85	−52.25	1	23.27	C
ATOM	333	O	PHE A	114	−7.637	15.86	−52.728	1	21.65	O
ATOM	334	CB	PHE A	114	−8.987	13.208	−52.582	1	23.69	C
ATOM	335	CG	PHE A	114	−9.683	11.983	−52.077	1	18.44	C
ATOM	336	CD1	PHE A	114	−10.811	12.092	−51.285	1	22.02	C
ATOM	337	CD2	PHE A	114	−9.19	10.723	−52.366	1	25.83	C
ATOM	338	CE1	PHE A	114	−11.447	10.964	−50.805	1	26.42	C
ATOM	339	CE2	PHE A	114	−9.821	9.592	−51.89	1	23.08	C
ATOM	340	CZ	PHE A	114	−10.949	9.712	−51.107	1	25.76	C
ATOM	341	H	PHE A	114	−9.255	14.925	−50.61	1	19.91	H
ATOM	342	HA	PHE A	114	−7.393	13.062	−51.305	1	24.52	H
ATOM	343	HB2	PHE A	114	−9.662	13.88	−52.767	1	28.43	H
ATOM	344	HB3	PHE A	114	−8.524	12.972	−53.401	1	28.43	H
ATOM	345	HD1	PHE A	114	−11.149	12.933	−51.079	1	26.43	H
ATOM	346	HD2	PHE A	114	−8.428	10.637	−52.893	1	31	H
ATOM	347	HE1	PHE A	114	−12.209	11.047	−50.278	1	31.7	H
ATOM	348	HE2	PHE A	114	−9.485	8.749	−52.095	1	27.69	H
ATOM	349	HZ	PHE A	114	−11.377	8.951	−50.787	1	30.91	H
ATOM	350	N	ASP A	115	−5.81	14.617	−52.275	1	21.39	N
ATOM	351	CA	ASP A	115	−4.861	15.629	−52.727	1	28.87	C
ATOM	352	C	ASP A	115	−4.607	15.563	−54.233	1	29.39	C
ATOM	353	O	ASP A	115	−3.87	16.383	−54.778	1	29.44	O
ATOM	354	CB	ASP A	115	−3.541	15.496	−51.959	1	30.8	C
ATOM	355	G	ASP A	115	−2.889	14.136	−52.135	1	36.31	C
ATOM	356	OD1	ASP A	115	−3.559	13.199	−52.615	1	34.47	O
ATOM	357	OD2	ASP A	115	−1.698	14.005	−51.78	1	46.52	O1−
ATOM	358	H	ASP A	115	−5.444	13.877	−52.034	1	25.67	H
ATOM	359	HA	ASP A	115	−5.228	16.505	−52.53	1	34.65	H
ATOM	360	HB2	ASP A	115	−2.921	16.169	−52.278	1	36.95	H
ATOM	361	HB3	ASP A	115	−3.713	15.625	−51.013	1	36.95	H
ATOM	362	N	GLU A	116	−5.226	14.596	−54.903	1	28.73	N
ATOM	363	CA	GLU A	116	−5.17	14.52	−56.362	1	33.21	C
ATOM	364	C	GLU A	116	−6.288	15.378	−56.938	1	33.91	C
ATOM	365	O	GLU A	116	−7.466	15.116	−56.699	1	38.64	O
ATOM	366	CB	GLU A	116	−5.287	13.075	−56.86	1	37.54	C
ATOM	367	CG	GLU A	116	−6.251	12.196	−56.072	1	39.66	C
ATOM	368	CD	GLU A	116	−5.606	11.573	−54.842	1	41.78	C
ATOM	369	OE1	GLU A	116	−4.525	10.959	−54.979	1	47.28	O
ATOM	370	OE2	GLU A	116	−6.177	11.707	−53.737	1	32.41	O1−
ATOM	371	H	GLU A	116	−5.687	13.969	−54.536	1	34.48	H
ATOM	372	HA	GLU A	116	−4.323	14.88	−56.669	1	39.85	H
ATOM	373	HB2	GLU A	116	−5.592	13.09	−57.781	1	45.05	H
ATOM	374	HB3	GLU A	116	−4.411	12.662	−56.815	1	45.05	H
ATOM	375	HG2	GLU A	116	−7.001	12.735	−55.777	1	47.6	H
ATOM	376	HG3	GLU A	116	−6.563	11.477	−56.643	1	47.6	H
ATOM	377	N	SER A	117	−5.915	16.408	−57.69	1	24.41	N
ATOM	378	CA	SER A	117	−6.878	17.401	−58.14	1	29.4	C
ATOM	379	C	SER A	117	−7.682	16.92	−59.344	1	31.91	C
ATOM	380	O	SER A	117	−7.135	16.366	−60.296	1	31.79	O
ATOM	381	CB	SER A	117	−6.169	18.715	−58.475	1	29.88	C
ATOM	382	OG	SER A	117	−5.324	18.57	−59.597	1	37.03	O
ATOM	383	H	SER A	117	−5.109	16.553	−57.953	1	29.3	H
ATOM	384	HA	SER A	117	−7.502	17.578	−57.419	1	35.28	H
ATOM	385	HB2	SER A	117	−6.836	19.392	−58.669	1	35.86	H
ATOM	386	HB3	SER A	117	−5.634	18.987	−57.712	1	35.86	H
ATOM	387	HG	SER A	117	−4.943	19.299	−59.767	1	44.43	H
ATOM	388	N	LYS A	118	−8.992	17.136	−59.276	1	27.54	N
ATOM	389	CA	LYS A	118	−9.912	16.776	−60.348	1	27.36	C
ATOM	390	C	LYS A	118	−10.967	17.859	−60.482	1	25.25	C
ATOM	391	O	LYS A	118	−11.153	18.661	−59.564	1	21.89	O
ATOM	392	CB	LYS A	118	−10.586	15.433	−60.07	1	24.18	C
ATOM	393	CG	LYS A	118	−9.635	14.268	−59.906	1	30.02	C
ATOM	394	CD	LYS A	118	−10.378	12.951	−60.041	1	32.21	C
ATOM	395	CE	LYS A	118	−9.457	11.767	−59.823	1	34.89	C
ATOM	396	NZ	LYS A	118	−9.058	11.664	−58.403	1	38.04	N1+
ATOM	397	H	LYS A	118	−9.381	17.499	−58.6	1	33.04	H
ATOM	398	HA	LYS A	118	−9.427	16.712	−61.185	1	32.84	H
ATOM	399	HB2	LYS A	118	−11.1	15.508	−59.252	1	29.02	H
ATOM	400	HB3	LYS A	118	−11.178	15.225	−60.81	1	29.02	H
ATOM	401	HG2	LYS A	118	−8.953	14.308	−60.595	1	36.02	H
ATOM	402	HG3	LYS A	118	−9.23	14.303	−59.025	1	36.02	H
ATOM	403	HD2	LYS A	118	−11.085	12.913	−59.378	1	38.65	H
ATOM	404	HD3	LYS A	118	−10.752	12.885	−60.934	1	38.65	H
ATOM	405	HE2	LYS A	118	−9.918	10.95	−60.071	1	41.87	H
ATOM	406	HE3	LYS A	118	−8.656	11.879	−60.358	1	41.87	H
ATOM	407	HZ1	LYS A	118	−9.779	11.559	−57.891	1	45.64	H
ATOM	408	HZ2	LYS A	118	−8.518	10.966	−58.288	1	45.64	H
ATOM	409	HZ3	LYS A	118	−8.631	12.404	−58.152	1	45.64	H
ATOM	410	N	ASN A	119	−11.664	17.885	−61.612	1	23.33	N
ATOM	411	CA	ASN A	119	−12.769	18.818	−61.77	1	22.32	C
ATOM	412	C	ASN A	119	−13.904	18.37	−60.861	1	18.79	C
ATOM	413	O	ASN A	119	−13.846	17.281	−60.292	1	20.16	O
ATOM	414	CB	ASN A	119	−13.213	18.92	−63.235	1	26.91	C
ATOM	415	CG	ASN A	119	−13.744	17.612	−63.795	1	27.14	C
ATOM	416	OD1	ASN A	119	−14.413	16.842	−63.11	1	23.11	O
ATOM	417	ND2	ASN A	119	−13.453	17.366	−65.066	1	29.78	N
ATOM	418	H	ASN A	119	−11.52	17.38	−62.293	1	27.99	H
ATOM	419	HA	ASN A	119	−12.483	19.699	−61.481	1	26.78	H
ATOM	420	HB2	ASN A	119	−13.919	19.582	−63.304	1	32.29	H
ATOM	421	HB3	ASN A	119	−12.454	19.189	−63.775	1	32.29	H
ATOM	422	HD21	ASN A	119	−13.728	16.641	−65.437	1	35.74	H
ATOM	423	HD22	ASN A	119	−12.99	17.932	−65.518	1	35.74	H
ATOM	424	N	TRP A	120	−14.925	19.204	−60.713	1	19	N
ATOM	425	CA	TRP A	120	−15.991	18.921	−59.76	1	20.49	C
ATOM	426	C	TRP A	120	−16.696	17.599	−60.061	1	22.8	C
ATOM	427	O	TRP A	120	−16.99	16.822	−59.15	1	19.34	O
ATOM	428	CB	TRP A	120	−17.014	20.055	−59.746	1	21.71	C
ATOM	429	CG	TRP A	120	−18.043	19.878	−58.679	1	20.57	C
ATOM	430	CD1	TRP A	120	−17.954	20.29	−57.382	1	20.1	C
ATOM	431	CD2	TRP A	120	−19.313	19.229	−58.808	1	20.41	C
ATOM	432	NE1	TRP A	120	−19.092	19.944	−56.696	1	18.87	N
ATOM	433	CE2	TRP A	120	−19.942	19.29	−57.548	1	21.17	C
ATOM	434	CE3	TRP A	120	−19.978	18.602	−59.865	1	22.6	C
ATOM	435	CZ2	TRP A	120	−21.205	18.749	−57.316	1	22.12	C
ATOM	436	CZ3	TRP A	120	−21.23	18.065	−59.635	1	20.75	C
ATOM	437	CH2	TRP A	120	−21.832	18.142	−58.371	1	28.09	C
ATOM	438	H	TRP A	120	−15.025	19.938	−61.149	1	22.8	H
ATOM	439	HA	TRP A	120	−15.606	18.856	−58.872	1	24.58	H
ATOM	440	HB2	TRP A	120	−16.555	20.894	−59.586	1	26.06	H
ATOM	441	HB3	TRP A	120	−17.47	20.082	−60.602	1	26.06	H
ATOM	442	HD1	TRP A	120	−17.23	20.744	−57.017	1	24.12	H
ATOM	443	HE1	TRP A	120	−19.246	20.11	−55.866	1	22.64	H
ATOM	444	HE3	TRP A	120	−19.585	18.546	−60.706	1	27.12	H
ATOM	445	HZ2	TRP A	120	−21.607	18.799	−56.479	1	26.54	H
ATOM	446	HZ3	TRP A	120	−21.683	17.647	−60.331	1	24.9	H
ATOM	447	HH2	TRP A	120	−22.677	17.774	−58.246	1	33.71	H
ATOM	448	N	TYR A	121	−16.96	17.346	−61.339	1	21.32	N
ATOM	449	CA	TYR A	121	−17.709	16.158	−61.743	1	25.07	C
ATOM	450	C	TYR A	121	−16.927	14.885	−61.415	1	20.81	C
ATOM	451	O	TYR A	121	−17.473	13.937	−60.848	1	21.52	O
ATOM	452	CB	TYR A	121	−18.037	16.221	−63.238	1	23.23	C
ATOM	453	CG	TYR A	121	−18.622	17.55	−63.662	1	26.15	C
ATOM	454	CD1	TYR A	121	−19.935	17.885	−63.353	1	33.8	C
ATOM	455	CD2	TYR A	121	−17.859	18.473	−64.363	1	24.99	C
ATOM	456	CE1	TYR A	121	−20.471	19.105	−63.734	1	30.23	C
ATOM	457	CE2	TYR A	121	−18.386	19.693	−64.748	1	33.24	C
ATOM	458	CZ	TYR A	121	−19.689	20.003	−64.431	1	29.9	C
ATOM	459	OH	TYR A	121	−20.21	21.217	−64.815	1	39.68	O
ATOM	460	H	TYR A	121	−16.717	17.848	−61.993	1	25.59	H
ATOM	461	HA	TYR A	121	−18.546	16.13	−61.254	1	30.08	H
ATOM	462	HB2	TYR A	121	−17.222	16.079	−63.745	1	27.87	H
ATOM	463	HB3	TYR A	121	−18.683	15.529	−63.448	1	27.87	H
ATOM	464	HD1	TYR A	121	−20.462	17.281	−62.882	1	40.56	H
ATOM	465	HD2	TYR A	121	−16.978	18.268	−64.578	1	29.99	H
ATOM	466	HE1	TYR A	121	−21.351	19.317	−63.521	1	36.27	H
ATOM	467	HE2	TYR A	121	−17.862	20.301	−65.218	1	39.89	H
ATOM	468	HH	TYR A	121	−21.008	21.28	−64.562	1	47.62	H
ATOM	469	N	GLU A	122	−15.645	14.883	−61.76	1	20.76	N
ATOM	470	CA	GLU A	122	−14.76	13.767	−61.449	1	22.88	C
ATOM	471	C	GLU A	122	−14.653	13.563	−59.938	1	22.74	C
ATOM	472	O	GLU A	122	−14.647	12.432	−59.451	1	21.61	O
ATOM	473	CB	GLU A	122	−13.374	14.011	−62.049	1	30.2	C
ATOM	474	CG	GLU A	122	−13.32	13.954	−63.575	1	37.52	C
ATOM	475	CD	GLU A	122	−11.969	14.386	−64.136	1	47.14	C
ATOM	476	OE1	GLU A	122	−11.248	15.152	−63.458	1	45.66	O
ATOM	477	OE2	GLU A	122	−11.625	13.956	−65.257	1	59.27	O1−
ATOM	478	H	GLU A	122	−15.258	15.525	−62.18	1	24.92	H
ATOM	479	HA	GLU A	122	−15.121	12.956	−61.839	1	27.46	H
ATOM	480	HB2	GLU A	122	−13.07	14.891	−61.777	1	36.24	H
ATOM	481	HB3	GLU A	122	−12.766	13.337	−61.708	1	36.24	H
ATOM	482	HG2	GLU A	122	−13.487	13.042	−63.863	1	45.03	H
ATOM	483	HG3	GLU A	122	−13.998	14.545	−63.937	1	45.03	H
ATOM	484	N	SER A	123	−14.565	14.666	−59.202	1	22.3	N
ATOM	485	CA	SER A	123	−14.528	14.613	−57.745	1	20.93	C
ATOM	486	C	SER A	123	−15.806	13.978	−57.214	1	20.42	C
ATOM	487	O	SER A	123	−15.762	13.104	−56.344	1	18.79	O
ATOM	488	CB	SER A	123	−14.345	16.015	−57.155	1	20.25	C
ATOM	489	OG	SER A	123	−13.11	16.585	−57.557	1	15.46	O
ATOM	490	H	SER A	123	−14.526	15.463	−59.524	1	26.76	H
ATOM	491	HA	SER A	123	−13.778	14.066	−57.465	1	25.12	H
ATOM	492	HB2	SER A	123	−15.069	16.583	−57.463	1	24.31	H
ATOM	493	HB3	SER A	123	−14.363	15.953	−56.187	1	24.31	H
ATOM	494	HG	SER A	123	−13.08	16.645	−58.395	1	18.56	H
ATOM	495	N	GLN A	124	−16.941	14.421	−57.749	1	19.5	N
ATOM	496	CA	GLN A	124	−18.241	13.88	−57.365	1	18.56	C
ATOM	497	C	GLN A	124	−18.3	12.38	−57.618	1	21.42	C
ATOM	498	O	GLN A	124	−18.736	11.612	−56.758	1	18.75	O
ATOM	499	CB	GLN A	124	−19.363	14.585	−58.134	1	22.37	C
ATOM	500	CG	GLN A	124	−20.744	13.971	−57.944	1	25.68	C
ATOM	501	CD	GLN A	124	−21.805	14.643	−58.8	1	30.6	C
ATOM	502	OE1	GLN A	124	−21.672	14.729	−60.023	1	32.6	O
ATOM	503	NE2	GLN A	124	−22.862	15.13	−58.159	1	27.2	N
ATOM	504	H	GLN A	124	−16.985	15.041	−58.344	1	23.4	H
ATOM	505	HA	GLN A	124	−18.382	14.033	−56.418	1	22.27	H
ATOM	506	HB2	GLN A	124	−19.408	15.508	−57.839	1	26.84	H
ATOM	507	HB3	GLN A	124	−19.156	14.555	−59.082	1	26.84	H
ATOM	508	HG2	GLN A	124	−20.71	13.033	−58.189	1	30.82	H
ATOM	509	HG3	GLN A	124	−21.006	14.062	−57.014	1	30.82	H
ATOM	510	HE21	GLN A	124	−23.489	15.52	−58.599	1	32.63	H
ATOM	511	HE22	GLN A	124	−22.918	15.055	−57.305	1	32.63	H
ATOM	512	N	ALA A	125	−17.868	11.972	−58.807	1	21.97	N
ATOM	513	CA	ALA A	125	−17.868	10.561	−59.176	1	20.84	C
ATOM	514	C	ALA A	125	−16.946	9.762	−58.26	1	21.56	C
ATOM	515	O	ALA A	125	−17.233	8.613	−57.929	1	23.96	O
ATOM	516	CB	ALA A	125	−17.448	10.394	−60.623	1	22.81	C
ATOM	517	H	ALA A	125	−17.569	12.494	−59.42	1	26.37	H
ATOM	518	HA	ALA A	125	−18.767	10.208	−59.081	1	25.01	H
ATOM	519	HB1	ALA A	125	−17.455	9.45	−60.846	1	27.37	H
ATOM	520	HB2	ALA A	125	−18.072	10.873	−61.19	1	27.37	H
ATOM	521	HB3	ALA A	125	−16.554	10.754	−60.735	1	27.37	H
ATOM	522	N	SER A	126	−15.841	10.38	−57.85	1	19.66	N
ATOM	523	CA	SER A	126	−14.891	9.726	−56.96	1	21.36	C
ATOM	524	C	SER A	126	−15.526	9.424	−55.597	1	20.78	C
ATOM	525	O	SER A	126	−15.4	8.316	−55.079	1	20.5	O
ATOM	526	CB	SER A	126	−13.644	10.595	−56.782	1	21.76	C
ATOM	527	OG	SER A	126	−12.641	9.91	−56.052	1	22.07	O
ATOM	528	H	SER A	126	−15.619	11.18	−58.074	1	23.59	H
ATOM	529	HA	SER A	126	−14.615	8.884	−57.355	1	25.64	H
ATOM	530	HB2	SER A	126	−13.294	10.826	−57.657	1	26.11	H
ATOM	531	HB3	SER A	126	−13.888	11.401	−56.301	1	26.11	H
ATOM	532	HG	SER A	126	−11.965	10.401	−55.964	1	26.49	H
ATOM	533	N	CYS A	127	−16.208	10.408	−55.018	1	17.68	N
ATOM	534	CA	CYS A	127	−16.855	10.214	−53.722	1	20.49	C
ATOM	535	C	CYS A	127	−17.995	9.206	−53.839	1	20.57	C
ATOM	536	O	CYS A	127	−18.171	8.348	−52.973	1	19.87	O
ATOM	537	CB	CYS A	127	−17.379	11.542	−53.174	1	18.87	C
ATOM	538	SG	CYS A	127	−16.086	12.764	−52.854	1	19.71	S
ATOM	539	H	CYS A	127	−16.312	11.193	−55.352	1	21.21	H
ATOM	540	HA	CYS A	127	−16.206	9.863	−53.092	1	24.59	H
ATOM	541	HB2	CYS A	127	−17.995	11.925	−53.818	1	22.65	H
ATOM	542	HB3	CYS A	127	−17.842	11.374	−52.337	1	22.65	H
ATOM	543	N	MET A	128	−18.765	9.315	−54.918	1	17.8	N
ATOM	544	CA	MET A	128	−19.856	8.382	−55.179	1	25.06	C
ATOM	545	C	MET A	128	−19.319	6.961	−55.283	1	22.86	C
ATOM	546	O	MET A	128	−19.956	6.008	−54.835	1	25.41	O
ATOM	547	CB	MET A	128	−20.593	8.754	−56.464	1	28.91	C
ATOM	548	CG	MET A	128	−22.085	8.97	−56.28	1	40.17	C
ATOM	549	SD	MET A	128	−22.957	9.136	−57.85	1	65.5	S
ATOM	550	CE	MET A	128	−22.156	10.582	−58.544	1	43.48	C
ATOM	551	H	MET A	128	−18.675	9.925	−55.518	1	21.37	H
ATOM	552	HA	MET A	128	−20.49	8.426	−54.447	1	30.08	H
ATOM	553	HB2	MET A	128	−20.216	9.577	−56.812	1	34.7	H
ATOM	554	HB3	MET A	128	−20.474	8.04	−57.11	1	34.7	H
ATOM	555	HG2	MET A	128	−22.459	8.21	−55.808	1	48.2	H
ATOM	556	HG3	MET A	128	−22.227	9.782	−55.769	1	48.2	H
ATOM	557	HE1	MET A	128	−22.549	10.776	−59.41	1	52.17	H
ATOM	558	HE2	MET A	128	−22.288	11.334	−57.945	1	52.17	H
ATOM	559	HE3	MET A	128	−21.208	10.401	−58.644	1	52.17	H
ATOM	560	N	SER A	129	−18.133	6.833	−55.865	1	22.61	N
ATOM	561	CA	SER A	129	−17.491	5.535	−56.033	1	26.16	C
ATOM	562	C	SER A	129	−17.085	4.913	−54.697	1	25.71	C
ATOM	563	O	SER A	129	−16.695	3.745	−54.645	1	24.09	O
ATOM	564	CB	SER A	129	−16.261	5.674	−56.935	1	25.52	C
ATOM	565	OG	SER A	129	−15.546	4.455	−57.022	1	33.82	O
ATOM	566	H	SER A	129	−17.673	7.491	−56.175	1	27.13	H
ATOM	567	HA	SER A	129	−18.113	4.93	−56.467	1	31.39	H
ATOM	568	HB2	SER A	129	−16.551	5.932	−57.824	1	30.62	H
ATOM	569	HB3	SER A	129	−15.677	6.355	−56.567	1	30.62	H
ATOM	570	HG	SER A	129	−16.039	3.855	−57.341	1	40.59	H
ATOM	571	N	GLN A	130	−17.171	5.694	−53.623	1	20.18	N
ATOM	572	CA	GLN A	130	−16.753	5.233	−52.303	1	22.43	C
ATOM	573	C	GLN A	130	−17.916	5.241	−51.317	1	24.16	C
ATOM	574	O	GLN A	130	−17.715	5.372	−50.111	1	27.76	O
ATOM	575	CB	GLN A	130	−15.612	6.103	−51.779	1	23.18	C
ATOM	576	CG	GLN A	130	−14.386	6.095	−52.674	1	25.86	C
ATOM	577	CD	GLN A	130	−13.321	7.067	−52.215	1	22.81	C
ATOM	578	OE1	GLN A	130	−12.837	6.988	−51.087	1	19.87	O
ATOM	579	NE2	GLN A	130	−12.951	7.993	−53.091	1	20.58	N
ATOM	580	H	GLN A	130	−17.47	6.5	−53.634	1	24.21	H
ATOM	581	HA	GLN A	130	−16.427	4.322	−52.375	1	26.92	H
ATOM	582	HB2	GLN A	130	−15.923	7.019	−51.709	1	27.81	H
ATOM	583	HB3	GLN A	130	−15.345	5.778	−50.905	1	27.81	H
ATOM	584	HG2	GLN A	130	−14.001	5.205	−52.674	1	31.04	H
ATOM	585	HG3	GLN A	130	−14.65	6.342	−53.574	1	31.04	H
ATOM	586	HE21	GLN A	130	−12.349	8.569	−52.879	1	24.7	H
ATOM	587	HE22	GLN A	130	−13.313	8.016	−53.871	1	24.7	H
ATOM	588	N	ASN A	131	−19.127	5.083	−51.839	1	23.03	N
ATOM	589	CA	ASN A	131	−20.331	5.118	−51.016	1	28.97	C
ATOM	590	C	ASN A	131	−20.37	6.396	−50.19	1	27.25	C
ATOM	591	O	ASN A	131	−20.655	6.375	−48.992	1	24.85	O
ATOM	592	CB	ASN A	131	−20.396	3.89	−50.104	1	30.97	C
ATOM	593	CG	ASN A	131	−21.744	3.736	−49.429	1	34.4	C
ATOM	594	OD1	ASN A	131	−22.772	4.158	−49.962	1	38.37	O
ATOM	595	ND2	ASN A	131	−21.745	3.139	−48.241	1	40.3	N
ATOM	596	H	ASN A	131	−19.28	4.953	−52.676	1	27.63	H
ATOM	597	HA	ASN A	131	−21.111	5.107	−51.593	1	34.76	H
ATOM	598	HB2	ASN A	131	−20.232	3.093	−50.633	1	37.17	H
ATOM	599	HB3	ASN A	131	−19.721	3.973	−49.413	1	37.17	H
ATOM	600	HD21	ASN A	131	−22.485	3.028	−47.817	1	48.35	H
ATOM	601	HD22	ASN A	131	−21.006	2.864	−47.897	1	48.35	H
ATOM	602	N	ALA A	132	−20.066	7.51	−50.846	1	25.64	N
ATOM	603	CA	ALA A	132	−19.98	8.8	−50.181	1	21.88	C
ATOM	604	C	ALA A	132	−20.378	9.915	−51.139	1	21.78	C
ATOM	605	O	ALA A	132	−20.768	9.663	−52.277	1	22.4	O
ATOM	606	CB	ALA A	132	−18.57	9.026	−49.656	1	20.15	C
ATOM	607	H	ALA A	132	−19.903	7.543	−51.69	1	30.77	H
ATOM	608	HA	ALA A	132	−20.591	8.813	−49.428	1	26.25	H
ATOM	609	HB1	ALA A	132	−18.531	9.89	−49.217	1	24.18	H
ATOM	610	HB2	ALA A	132	−18.352	8.323	−49.025	1	24.18	H
ATOM	611	HB3	ALA A	132	−17.949	9.006	−50.401	1	24.18	H
ATOM	612	N	SER A	133	−20.27	11.151	−50.672	1	18.84	N
ATOM	613	CA	SER A	133	−20.529	12.309	−51.509	1	21.81	C
ATOM	614	C	SER A	133	−19.499	13.378	−51.19	1	19.07	C
ATOM	615	C	SER A	133	−18.693	13.211	−50.276	1	17.95	O
ATOM	616	CB	SER A	133	−21.945	12.833	−51.281	1	25.17	C
ATOM	617	OG	SER A	133	−22.071	13.372	−49.979	1	30.73	O
ATOM	618	H	SER A	133	−20.045	11.346	−49.865	1	22.61	H
ATOM	619	HA	SER A	133	−20.438	12.061	−52.442	1	26.18	H
ATOM	620	HB2	SER A	133	−22.134	13.528	−51.931	1	30.2	H
ATOM	621	HB3	SER A	133	−22.574	12.102	−51.384	1	30.2	H
ATOM	622	HG	SER A	133	−21.908	12.78	−49.406	1	36.88	H
ATOM	623	N	LEU A	134	−19.516	14.469	−51.947	1	18.66	N
ATOM	624	CA	LEU A	134	−18.644	15.594	−51.646	1	18.37	C
ATOM	625	C	LEU A	134	−19.076	16.218	−50.327	1	17.9	C
ATOM	626	O	LEU A	134	−20.216	16.046	−49.898	1	17.3	O
ATOM	627	CB	LEU A	134	−18.675	16.627	−52.772	1	17.75	C
ATOM	628	CG	LEU A	134	−17.977	16.21	−54.067	1	16.83	C
ATOM	629	CD1	LEU A	134	−18.32	17.168	−55.192	1	18.55	C
ATOM	630	CD2	LEU A	134	−16.469	16.142	−53.878	1	18.53	C
ATOM	631	H	LEU A	134	−20.019	14.581	−52.635	1	22.4	H
ATOM	632	HA	LEU A	134	−17.733	15.276	−51.549	1	22.05	H
ATOM	633	HB2	LEU A	134	−19.601	16.817	−52.988	1	21.31	H
ATOM	634	HB3	LEU A	134	−18.243	17.436	−52.457	1	21.31	H
ATOM	635	HG	LEU A	134	−18.287	15.327	−54.322	1	20.2	H
ATOM	636	HD11	LEU A	134	−18.028	18.06	−54.946	1	22.26	H
ATOM	637	HD12	LEU A	134	−17.866	16.882	−56	1	22.26	H
ATOM	638	HD13	LEU A	134	−19.28	17.161	−55.331	1	22.26	H
ATOM	639	HD21	LEU A	134	−16.266	15.491	−53.188	1	22.24	H
ATOM	640	HD22	LEU A	134	−16.058	15.876	−54.716	1	22.24	H
ATOM	641	HD23	LEU A	134	−16.144	17.017	−53.613	1	22.24	H
ATOM	642	N	LEU A	135	−18.157	16.926	−49.681	1	15.27	N
ATOM	643	CA	LEU A	135	−18.428	17.543	−48.386	1	14.24	C
ATOM	644	C	LEU A	135	−19.756	18.295	−48.351	1	13.72	C
ATOM	645	O	LEU A	135	−20.021	19.141	−49.207	1	14.87	O
ATOM	646	CB	LEU A	135	−17.299	18.503	−48.018	1	11.92	C
ATOM	647	CG	LEU A	135	−17.524	19.369	−46.773	1	13.8	C
ATOM	648	CD1	LEU A	135	−17.707	18.499	−45.536	1	16.19	C
ATOM	649	CD2	LEU A	135	−16.366	20.34	−46.586	1	15.37	C
ATOM	650	H	LEU A	135	−17.361	17.065	−49.975	1	18.33	H
ATOM	651	HA	LEU A	135	−18.461	16.848	−47.71	1	17.09	H
ATOM	652	HB2	LEU A	135	−16.495	17.982	−47.865	1	14.3	H
ATOM	653	HB3	LEU A	135	−17.156	19.104	−48.765	1	14.3	H
ATOM	654	HG	LEU A	135	−18.333	19.889	−46.894	1	16.56	H
ATOM	655	HD11	LEU A	135	−17.846	19.072	−44.766	1	19.43	H
ATOM	656	HD12	LEU A	135	−18.477	17.924	−45.666	1	19.43	H
ATOM	657	HD13	LEU A	135	−16.91	17.961	−45.409	1	19.43	H
ATOM	658	HD21	LEU A	135	−16.529	20.877	−45.795	1	18.45	H
ATOM	659	HD22	LEU A	135	−15.545	19.835	−46.48	1	18.45	H
ATOM	660	HD23	LEU A	135	−16.305	20.912	−47.367	1	18.45	H
ATOM	661	N	LYS A	136	−20.583	17.967	−47.359	1	11.97	N
ATOM	662	CA	LYS A	136	−21.789	18.732	−47.064	1	19.27	C
ATOM	663	C	LYS A	136	−21.649	19.428	−45.714	1	16.87	C
ATOM	664	O	LYS A	136	−21.409	18.784	−44.691	1	16.35	O
ATOM	665	CB	LYS A	136	−23.029	17.836	−47.062	1	20.92	C
ATOM	666	CG	LYS A	136	−24.294	18.572	−46.624	1	23.85	C
ATOM	667	CD	LYS A	136	−25.542	17.721	−46.767	1	27.86	C
ATOM	668	CE	LYS A	136	−26.766	18.475	−46.263	1	36.34	C
ATOM	669	NZ	LYS A	136	−28.041	17.844	−46.689	1	34.12	N1+
ATOM	670	H	LYS A	136	−20.463	17.295	−46.836	1	14.37	H
ATOM	671	HA	LYS A		136	−21.908	19.412	−47.745	1	23.12	H
ATOM	672	HB2	LYS A	136	−23.176	17.498	−47.959	1	25.11	H
ATOM	673	HB3	LYS A	136	−22.885	17.099	−46.448	1	25.11	H
ATOM	674	HG2	LYS A		136	−24.207	18.824	−45.691	1	28.62	H
ATOM	675	HG3	LYS A		136	−24.406	19.364	−47.172	1	28.62	H
ATOM	676	HD2	LYS A		136	−25.679	17.503	−47.702	1	33.44	H
ATOM	677	HD3	LYS A		136	−25.443	16.912	−46.241	1	33.44	H
ATOM	678	HE2	LYS A		136	−26.749	18.494	−45.294	1	43.61	H
ATOM	679	HE3	LYS A		136	−26.746	19.379	−46.614	1	43.61	H
ATOM	680	HZ1	LYS A		136	−28.73	18.312	−46.377	1	40.94	H
ATOM	681	HZ2	LYS A	136	−28.086	17.82	−47.577	1	40.94	H
ATOM	682	HZ3	LYS A	136	−28.088	17.013	−46.374	1	40.94	H
ATOM	683	N	VAL A		137	−21.807	20.746	−45.726	1	17.32	N
ATOM	684	CA	VAL A		137	−21.728	21.552	−44.516	1	16.33	C
ATOM	685	C	VAL A		137	−23.137	21.792	−43.974	1	18.35	C
ATOM	686	O	VAL A	137	−23.93	22.488	−44.603	1	20.87	O
ATOM	687	CB	VAL A	137	−21.028	22.895	−44.788	1	17.82	C
ATOM	688	CG1	VAL A	137	−20.955	23.732	−43.518	1	22.96	C
ATOM	689	CG2	VAL A	137	−19.627	22.656	−45.354	1	18.45	C
ATOM	690	H	VAL A		137	−21.964	21.205	−46.436	1	20.78	H
ATOM	691	HA	VAL A		137	−21.22	21.073	−43.843	1	19.6	H
ATOM	692	HB	VAL A	137	−21.539	23.391	−45.447	1	21.39	H
ATOM	693	HG11	VAL A	137	−20.51	24.571	−43.719	1	27.55	H
ATOM	694	HG12	VAL A	137	−21.856	23.903	−43.201	1	27.55	H
ATOM	695	HG13	VAL A	137	−20.454	23.244	−42.847	1	27.55	H
ATOM	696	HG21	VAL A	137	−19.203	23.513	−45.519	1	22.14	H
ATOM	697	HG22	VAL A	137	−19.109	22.148	−44.711	1	22.14	H
ATOM	698	HG23	VAL A	137	−19.703	22.159	−46.184	1	22.14	H
ATOM	699	N	TYR A	138	−23.437	21.22	−42.81	1	19.32	N
ATOM	700	CA	TYR A	138	−24.792	21.266	−42.259	1	24.49	C
ATOM	701	C	TYR A	138	−24.832	21.797	−40.83	1	24.58	C
ATOM	702	O	TYR A	138	−25.909	22.078	−40.302	1	22.3	O
ATOM	703	CB	TYR A	138	−25.423	19.871	−42.295	1	21.46	C
ATOM	704	CG	TYR A	138	−24.849	18.919	−41.271	1	22.69	C
ATOM	705	CD1	TYR A	138	−23.689	18.203	−41.533	1	21.21	C
ATOM	706	CD2	TYR A	138	−25.463	18.742	−40.037	1	22.66	C
ATOM	707	CE1	TYR A	138	−23.16	17.331	−40.598	1	19.74	C
ATOM	708	CE2	TYR A	138	−24.94	17.874	−39.095	1	23.87	C
ATOM	709	CZ	TYR A	138	−23.788	17.172	−39.38	1	23.25	C
ATOM	710	OH	TYR A	138	−23.263	16.308	−38.446	1	19.45	O
ATOM	711	H	TYR A	138	−22.873	20.797	−42.318	1	23.18	H
ATOM	712	HA	TYR A	138	−25.334	21.853	−42.809	1	29.39	H
ATOM	713	HB2	TYR A	138	−26.374	19.954	−42.123	1	25.75	H
ATOM	714	HB3	TYR A	138	−25.279	19.485	−43.173	1	25.75	H
ATOM	715	HD1	TYR A	138	−23.263	18.308	−42.353	1	25.45	H
ATOM	716	HD2	TYR A	138	−26.239	19.214	−39.842	1	27.2	H
ATOM	717	HE1	TYR A	138	−22.383	16.857	−40.788	1	23.69	H
ATOM	718	HE2	TYR A	138	−25.363	17.766	−38.274	1	28.64	H
ATOM	719	HH	TYR A	138	−23.74	16.308	−37.755	1	23.34	H
ATOM	720	N	SER A	139	−23.668	21.933	−40.202	1	16.32	N
ATOM	721	CA	SER A	139	−23.62	22.342	−38.802	1	22.45	C
ATOM	722	C	SER A	139	−22.28	22.946	−38.399	1	21.92	C
ATOM	723	O	SER A	139	−21.243	22.31	−38.547	1	20.19	O
ATOM	724	CB	SER A	139	−23.922	21.142	−37.908	1	20.56	C
ATOM	725	OG	SER A	139	−23.63	21.435	−36.555	1	23.25	O
ATOM	726	H	SER A	139	−22.899	21.796	−40.56	1	19.58	H
ATOM	727	HA	SER A	139	−24.306	23.01	−38.646	1	26.94	H
ATOM	728	HB2	SER A	139	−24.862	20.918	−37.987	1	24.67	H
ATOM	729	HB3	SER A	139	−23.377	20.391	−38.193	1	24.67	H
ATOM	730	HG	SER A	139	−23.799	20.768	−36.073	1	27.89	H
ATOM	731	N	LYS A	140	−22.304	24.164	−37.869	1	21.91	N
ATOM	732	CA	LYS A	140	−21.074	24.803	−37.417	1	22.19	C
ATOM	733	C	LYS A	140	−20.566	24.16	−36.132	1	22.96	C
ATOM	734	O	LYS A	140	−19.382	24.24	−35.823	1	23.93	O
ATOM	735	CB	LYS A	140	−21.28	26.304	−37.215	1	25.51	C
ATOM	736	CG	LYS A	140	−21.119	27.111	−38.497	1	26.71	C
ATOM	737	CD	LYS A	140	−21.243	28.605	−38.258	1	29.71	C
ATOM	738	CE	LYS A	140	−20.959	29.383	−39.534	1	30.52	C
ATOM	739	NZ	LYS A	140	−21.099	30.852	−39.352	1	46.5	N1+
ATOM	740	H	LYS A	140	−23.013	24.638	−37.76	1	26.29	H
ATOM	741	HA	LYS A	140	−20.392	24.686	−38.097	1	26.63	H
ATOM	742	HB2	LYS A	140	−22.177	26.456	−36.877	1	30.61	H
ATOM	743	HB3	LYS A	140	−20.627	26.628	−36.574	1	30.61	H
ATOM	744	HG2	LYS A	140	−20.242	26.938	−38.873	1	32.06	H
ATOM	745	HG3	LYS A	140	−21.809	26.848	−39.126	1	32.06	H
ATOM	746	HD2	LYS A	140	−22.145	28.811	−37.969	1	35.66	H
ATOM	747	HD3	LYS A	140	−20.601	28.877	−37.584	1	35.66	H
ATOM	748	HE2	LYS A	140	−20.049	29.201	−39.819	1	36.62	H
ATOM	749	HE3	LYS A	140	−21.584	29.104	−40.22	1	36.62	H
ATOM	750	HZ1	LYS A	140	−20.925	31.271	−40.118	1	55.8	H
ATOM	751	HZ2	LYS A	140	−21.928	31.049	−39.097	1	55.8	H
ATOM	752	HZ3	LYS A	140	−20.529	31.138	−38.731	1	55.8	H
ATOM	753	N	GLU A	141	−21.459	23.513	−35.39	1	22.3	N
ATOM	754	CA	GLU A	141	−21.065	22.818	−34.17	1	22.51	C
ATOM	755	C	GLU A	141	−20.504	21.427	−34.473	1	23.38	C
ATOM	756	O	GLU A	141	−19.397	21.093	−34.048	1	20.37	O
ATOM	757	CB	GLU A	141	−22.25	22.705	−33.215	1	27.68	C
ATOM	758	CG	GLU A	141	−21.925	22.006	−31.91	1	37.33	C
ATOM	759	CD	GLU A	141	−23.137	21.869	−31.013	1	48.81	C
ATOM	760	OE1	GLU A	141	−23.28	22.685	−30.079	1	53.5	O
ATOM	761	OE2	GLU A	141	−23.95	20.947	−31.241	1	51.65	O1−
ATOM	762	H	GLU A	141	−22.298	23.461	−35.571	1	26.77	H
ATOM	763	HA	GLU A	141	−20.37	23.33	−33.727	1	27.01	H
ATOM	764	HB2	GLU A	141	−22.565	23.598	−33.003	1	33.21	H
ATOM	765	HB3	GLU A	141	−22.956	22.203	−33.652	1	33.21	H
ATOM	766	HG2	GLU A	141	−21.589	21.116	−32.101	1	44.8	H
ATOM	767	HG3	GLU A	141	−21.254	22.52	−31.433	1	44.8	H
ATOM	768	N	ASP A	142	−21.273	20.619	−35.2	1	22.34	N
ATOM	769	CA	ASP A	142	−20.873	19.244	−35.515	1	21.81	C
ATOM	770	C	ASP A	142	−19.649	19.185	−36.433	1	18.46	C
ATOM	771	O	ASP A	142	−18.949	18.171	−36.48	1	19.9	O
ATOM	772	CB	ASP A	142	−22.029	18.486	−36.178	1	21.93	C
ATOM	773	CG	ASP A	142	−23.054	17.966	−35.18	1	25.65	C
ATOM	774	OD1	ASP A	142	−23.061	18.415	−34.015	1	31.16	O
ATOM	775	OD2	ASP A	142	−23.865	17.101	−35.576	1	29.49	O1−
ATOM	776	H	ASP A	142	−22.037	20.843	−35.526	1	26.8	H
ATOM	777	HA	ASP A	142	−20.649	18.786	−34.69	1	26.17	H
ATOM	778	HB2	ASP A	142	−22.485	19.082	−36.792	1	26.32	H
ATOM	779	HB3	ASP A	142	−21.67	17.725	−36.661	1	26.32	H
ATOM	780	N	GLN A	143	−19.407	20.265	−37.169	1	17.54	N
ATOM	781	CA	GLN A	143	−18.302	20.325	−38.124	1	18.55	C
ATOM	782	C	GLN A	143	−17.408	21.528	−37.839	1	21.09	C
ATOM	783	O	GLN A	143	−16.838	22.123	−38.756	1	15.66	O
ATOM	784	CB	GLN A	143	−18.842	20.393	−39.553	1	17.56	C
ATOM	785	CG	GLN A	143	−19.803	19.267	−39.896	1	20.23	C
ATOM	786	CD	GLN A	143	−20.459	19.445	−41.251	1	20.71	C
ATOM	787	OE1	GLN A	143	−21.171	20.425	−41.486	1	19.03	O
ATOM	788	NE2	GLN A	143	−20.225	18.496	−42.152	1	18.38	N
ATOM	789	H	GLN A	143	−19.874	20.986	−37.134	1	21.05	H
ATOM	790	HA	GLN A	143	−17.765	19.521	−38.041	1	22.26	H
ATOM	791	HB2	GLN A	143	−19.314	21.232	−39.67	1	21.08	H
ATOM	792	HB3	GLN A	143	−18.096	20.345	−40.172	1	21.08	H
ATOM	793	HG2	GLN A	143	−19.315	18.428	−39.907	1	24.27	H
ATOM	794	HG3	GLN A	143	−20.503	19.234	−39.226	1	24.27	H
ATOM	795	HE21	GLN A	143	−20.574	18.552	−42.935	1	22.06	H
ATOM	796	HE22	GLN A	143	−19.724	17.827	−41.95	1	22.06	H
ATOM	797	N	ASP A	144	−17.288	21.876	−36.561	1	17.64	N
ATOM	798	CA	ASP A	144	−16.568	23.078	−36.157	1	19.87	C
ATOM	799	C	ASP A	144	−15.114	23.071	−36.621	1	19.55	C
ATOM	800	O	ASP A	144	−14.547	24.122	−36.92	1	19.43	O
ATOM	801	CB	ASP A	144	−16.632	23.247	−34.636	1	21.16	C
ATOM	802	CG	ASP A	144	−16.132	22.027	−33.882	1	25.44	C
ATOM	803	OD1	ASP A	144	−16.127	20.917	−34.455	1	24.83	O
ATOM	804	OD2	ASP A	144	−15.753	22.181	−32.702	1	30.53	O1−
ATOM	805	H	ASP A	144	−17.618	21.429	−35.904	1	21.16	H
ATOM	806	HA	ASP A	144	−17.001	23.848	−36.558	1	23.85	H
ATOM	807	HB2	ASP A	144	−16.081	24.004	−34.38	1	25.4	H
ATOM	808	HB3	ASP A	144	−17.552	23.405	−34.374	1	25.4	H
ATOM	809	N	LEU A	145	−14.516	21.891	−36.711	1	17.05	N
ATOM	810	CA	LEU A	145	−13.098	21.807	−37.047	1	17.13	C
ATOM	811	C	LEU A	145	−12.832	22.091	−38.531	1	17.51	C
ATOM	812	O	LEU A	145	−11.681	22.142	−38.963	1	18.01	O
ATOM	813	CB	LEU A	145	−12.549	20.442	−36.639	1	22.72	C
ATOM	814	CG	LEU A	145	−12.526	20.245	−35.115	1	27.83	C
ATOM	815	CD1	LEU A	145	−12.087	18.841	−34.761	1	30.89	C
ATOM	816	CD2	LEU A	145	−11.61	21.254	−34.415	1	26.54	C
ATOM	817	H	LEU A	145	−14.9	21.132	−36.585	1	20.46	H
ATOM	818	HA	LEU A	145	−12.621	22.478	−36.533	1	20.56	H
ATOM	819	HB2	LEU A	145	−13.109	19.748	−37.023	1	27.26	H
ATOM	820	HB3	LEU A	145	−11.641	20.355	−36.967	1	27.26	H
ATOM	821	HG	LEU A	145	−13.424	20.371	−34.77	1	33.39	H
ATOM	822	HD11	LEU A	145	−12.082	18.746	−33.795	1	37.07	H
ATOM	823	HD12	LEU A	145	−12.709	18.208	−35.152	1	37.07	H
ATOM	824	HD13	LEU A	145	−11.196	18.691	−35.113	1	37.07	H
ATOM	825	HD21	LEU A	145	−11.63	21.089	−33.459	1	31.85	H
ATOM	826	HD22	LEU A	145	−10.706	21.145	−34.75	1	31.85	H
ATOM	827	HD23	LEU A	145	−11.927	22.151	−34.602	1	31.85	H
ATOM	828	N	LEU A	146	−13.892	22.317	−39.3	1	14.54	N
ATOM	829	CA	LEU A	146	−13.741	22.812	−40.663	1	17.73	C
ATOM	830	C	LEU A	146	−13.1	24.2	−40.661	1	13.72	C
ATOM	831	O	LEU A	146	−12.574	24.65	−41.679	1	14.63	O
ATOM	832	CB	LEU A	146	−15.093	22.857	−41.382	1	16.27	C
ATOM	833	CG	LEU A	146	−15.734	21.525	−41.77	1	19.7	C
ATOM	834	CD1	LEU A	146	−17.09	21.764	−42.414	1	16.79	C
ATOM	835	CD2	LEU A	146	−14.839	20.74	−42.715	1	17.92	C
ATOM	836	H	LEU A	146	−14.708	22.193	−39.057	1	17.45	H
ATOM	837	HA	LEU A	146	−13.158	22.212	−41.155	1	21.28	H
ATOM	838	HB2	LEU A	146	−15.723	23.318	−40.806	1	19.52	H
ATOM	839	HB3	LEU A	146	−14.98	23.366	−42.2	1	19.52	H
ATOM	840	HG	LEU A	146	−15.869	20.992	−40.971	1	23.64	H
ATOM	841	HD11	LEU A	146	−17.481	20.909	−42.653	1	20.15	H
ATOM	842	HD12	LEU A	146	−17.663	22.224	−41.782	1	20.15	H
ATOM	843	HD13	LEU A	146	−16.97	22.307	−43.209	1	20.15	H
ATOM	844	HD21	LEU A	146	−15.275	19.903	−42.94	1	21.5	H
ATOM	845	HD22	LEU A	146	−14.692	21.264	−43.518	1	21.5	H
ATOM	846	HD23	LEU A	146	−13.992	20.565	−42.275	1	21.5	H
ATOM	847	N	LYS A	147	−13.14	24.875	−39.517	1	15.29	N
ATOM	848	CA	LYS A	147	−12.485	26.173	−39.36	1	18.16	C
ATOM	849	C	LYS A	147	−10.973	26.053	−39.545	1	16.32	C
ATOM	850	O	LYS A	147	−10.321	26.979	−40.029	1	15.57	O
ATOM	851	CB	LYS A	147	−12.798	26.763	−37.981	1	22.56	C
ATOM	852	CG	LYS A	147	−12.018	28.031	−37.645	1	33.54	C
ATOM	853	CD	LYS A	147	−12.43	28.588	−36.287	1	49.3	C
ATOM	854	CE	LYS A	147	−11.588	29.796	−35.894	1	57.42	C
ATOM	855	NZ	LYS A	147	−11.76	30.941	−36.829	1	59.81	N1+
ATOM	856	H	LYS A	147	−13.544	24.601	−38.808	1	18.35	H
ATOM	857	HA	LYS A	147	−12.824	26.783	−40.034	1	21.79	H
ATOM	858	HB2	LYS A	147	−13.742	26.98	−37.943	1	27.07	H
ATOM	859	HB3	LYS A	147	−12.587	26.1	−37.305	1	27.07	H
ATOM	860	HG2	LYS A	147	−11.07	27.826	−37.616	1	40.24	H
ATOM	861	HG3	LYS A	147	−12.197	28.705	−38.318	1	40.24	H
ATOM	862	HD2	LYS A	147	−13.359	28.864	−36.324	1	59.16	H
ATOM	863	HD3	LYS A	147	−12.31	27.902	−35.612	1	59.16	H
ATOM	864	HE2	LYS A	147	−11.851	30.089	−35.008	1	68.91	H
ATOM	865	HE3	LYS A	147	−10.652	29.543	−35.897	1	68.91	H
ATOM	866	HZ1	LYS A	147	−11.255	31.626	−36.567	1	71.78	H
ATOM	867	HZ2	LYS A	147	−11.519	30.701	−37.652	1	71.78	H
ATOM	868	HZ3	LYS A	147	−12.612	31.199	−36.841	1	71.78	H
ATOM	869	N	LEU A	148	−10.426	24.903	−39.166	1	13.11	N
ATOM	870	CA	LEU A	148	−8.984	24.68	−39.204	1	13.14	C
ATOM	871	C	LEU A	148	−8.491	24.075	−40.519	1	13.81	C
ATOM	872	O	LEU A	148	−7.296	23.812	−40.667	1	17.85	O
ATOM	873	CB	LEU A	148	−8.568	23.765	−38.052	1	15.95	C
ATOM	874	CG	LEU A	148	−8.725	24.317	−36.634	1	20.41	C
ATOM	875	CD1	LEU A	148	−8.325	23.25	−35.63	1	17.28	C
ATOM	876	CD2	LEU A	148	−7.903	25.578	−36.435	1	21.97	C
ATOM	877	H	LEU A	148	−10.875	24.228	−38.879	1	15.73	H
ATOM	878	HA	LEU A	148	−8.534	25.531	−39.084	1	15.77	H
ATOM	879	HB2	LEU A	148	−9.099	22.954	−38.103	1	19.14	H
ATOM	880	HB3	LEU A	148	−7.631	23.54	−38.169	1	19.14	H
ATOM	881	HG	LEU A	148	−9.657	24.538	−36.482	1	24.49	H
ATOM	882	HD11	LEU A	148	−8.427	23.607	−34.733	1	20.73	H
ATOM	883	HD12	LEU A	148	−8.898	22.477	−35.746	1	20.73	H
ATOM	884	HD13	LEU A	148	7.4	23.003	−35.784	1	20.73	H
ATOM	885	HD21	LEU A	148	−8.028	25.897	−35.527	1	26.36	H
ATOM	886	HD22	LEU A	148	−6.967	25.372	−36.587	1	26.36	H
ATOM	887	HD23	LEU A	148	−8.2	26.252	−37.066	1	26.36	H
ATOM	888	N	VAL A	149	−9.396	23.849	−41.467	1	14.39	N
ATOM	889	CA	VAL A	149	−9.009	23.24	−42.738	1	13.95	C
ATOM	890	C	VAL A	149	−8.252	24.22	−43.624	1	15.01	C
ATOM	891	O	VAL A	149	−8.734	25.307	−43.936	1	13.43	O
ATOM	892	CB	VAL A	149	−10.234	22.703	−43.505	1	13.62	C
ATOM	893	CG1	VAL A	149	−9.869	22.333	−44.945	1	18.07	C
ATOM	894	CG2	VAL A	149	−10.796	21.498	−42.787	1	13.27	C
ATOM	895	H	VAL A		149	−10.233	24.036	−41.401	1	17.27	H
ATOM	896	HA	VAL A		149	−8.422	22.49	−42.557	1	16.74	H
ATOM	897	HB	VAL A	149	−10.92	23.388	−43.532	1	16.34	H
ATOM	898	HG11	VAL A	149	−10.661	22	−45.396	1	21.68	H
ATOM	899	HG12	VAL A	149	−9.537	23.123	−45.4	1	21.68	H
ATOM	900	HG13	VAL A	149	−9.184	21.646	−44.93	1	21.68	H
ATOM	901	HG21	VAL A	149	−11.566	21.169	−43.278	1	15.93	H
ATOM	902	HG22	VAL A	149	−10.113	20.811	−42.742	1	15.93	H
ATOM	903	HG23	VAL A	149	−11.062	21.76	−41.892	1	15.93	H
ATOM	904	N	LYS A	150	−7.063	23.797	−44.032	1	13.03	N
ATOM	905	CA	LYS A	150	−6.189	24.572	−44.898	1	14.72	C
ATOM	906	C	LYS A	150	−6.493	24.295	−46.366	1	13.85	C
ATOM	907	O	LYS A	150	−6.988	23.224	−46.705	1	15.19	O
ATOM	908	CB	LYS A	150	−4.73	24.229	−44.589	1	17.03	C
ATOM	909	CG	LYS A	150	−3.696	25.097	−45.282	1	16.21	C
ATOM	910	CD	LYS A	150	−2.302	24.647	−44.88	1	15.63	C
ATOM	911	CE	LYS A	150	−1.224	25.608	−45.344	1	20.81	C
ATOM	912	NZ	LYS A	150	0.121	25.154	−44.907	1	24.83	N1+
ATOM	913	H	LYS A	150	−6.729	23.036	−43.81	1	15.64	H
ATOM	914	HA	LYS A	150	−6.324	25.518	−44.73	1	17.66	H
ATOM	915	HB2	LYS A	150	−4.59	24.317	−43.633	1	20.44	H
ATOM	916	HB3	LYS A	150	−4.567	23.312	−44.857	1	20.44	H
ATOM	917	HG2	LYS A	150	−3.786	25.006	−46.243	1	19.45	H
ATOM	918	HG3	LYS A	150	−3.813	26.021	−45.013	1	19.45	H
ATOM	919	HD2	LYS A	150	−2.255	24.587	−43.913	1	18.76	H
ATOM	920	HD3	LYS A		150	−2.122	23.78	−45.276	1	18.76	H
ATOM	921	HE2	LYS A		150	−1.23	25.654	−46.313	1	24.98	H
ATOM	922	HE3	LYS A		150	−1.389	26.484	−44.964	1	24.98	H
ATOM	923	HZ1	LYS A	150	0.296	24.35	−45.246	1	29.79	H
ATOM	924	HZ2	LYS A	150	0.741	25.728	−45.186	1	29.79	H
ATOM	925	HZ3	LYS A	150	0.151	25.106	−44.018	1	29.79	H
ATOM	926	N	SER A	151	−6.191	25.271	−47.219	1	11.64	N
ATOM	927	CA	SER A	151	−6.34	25.146	−48.669	1	12	C
ATOM	928	C	SER A	151	−7.809	25.15	−49.09	1	15.77	C
ATOM	929	O	SER A	151	−8.698	25.423	−48.283	1	13.47	O
ATOM	930	CB	SER A	151	−5.657	23.875	−49.185	1	15.08	C
ATOM	931	OG	SER A	151	−5.545	23.9	−50.6	1	18.05	O
ATOM	932	H	SER A	151	−5.889	26.038	−46.975	1	13.97	H
ATOM	933	HA	SER A	151	−5.91	25.905	−49.092	1	14.4	H
ATOM	934	HB2	SER A	151	−4.769	23.815	−48.8	1	18.09	H
ATOM	935	HB3	SER A	151	−6.184	23.104	−48.924	1	18.09	H
ATOM	936	HG	SER A	151	−5.169	23.2	−50.871	1	21.66	H
ATOM	937	N	TYR A	152	−8.034	24.838	−50.363	1	15.37	N
ATOM	938	CA	TYR A	152	−9.332	24.985	−51.015	1	14.25	C
ATOM	939	C	TYR A	152	−9.729	23.674	−51.687	1	16.05	C
ATOM	940	O	TYR A	152	−8.929	23.071	−52.401	1	15.6	O
ATOM	941	CB	TYR A	152	−9.27	26.138	−52.025	1	15.37	C
ATOM	942	CG	TYR A	152	−8.986	27.455	−51.343	1	16.48	C
ATOM	943	CD1	TYR A	152	−7.721	27.747	−50.853	1	14.01	C
ATOM	944	CD2	TYR A	152	−9.991	28.393	−51.161	1	18.15	C
ATOM	945	CE1	TYR A	152	−7.464	28.935	−50.202	1	15.58	C
ATOM	946	CE2	TYR A	152	−9.745	29.584	−50.511	1	16.03	C
ATOM	947	CZ	TYR A	152	−8.48	29.85	−50.032	1	17.68	C
ATOM	948	OH	TYR A	152	−8.237	31.038	−49.385	1	16.49	O
ATOM	949	H	TYR A	152	−7.428	24.528	−50.888	1	18.44	H
ATOM	950	HA	TYR A	152	−10.003	25.2	−50.348	1	17.09	H
ATOM	951	HB2	TYR A	152	−8.56	25.967	−52.663	1	18.44	H
ATOM	952	HB3	TYR A	152	−10.123	26.21	−52.482	1	18.44	H
ATOM	953	HD1	TYR A	152	−7.036	27.127	−50.958	1	16.82	H
ATOM	954	HD2	TYR A	152	−10.847	28.212	−51.474	1	21.78	H
ATOM	955	HE1	TYR A	152	−6.611	29.117	−49.879	1	18.7	H
ATOM	956	HE2	TYR A	152	−10.428	30.204	−50.396	1	19.23	H
ATOM	957	HH	TYR A	152	−8.94	31.496	−49.353	1	19.79	H
ATOM	958	N	HIS A	153	−10.959	23.228	−51.441	1	16.84	N
ATOM	959	CA	HIS A	153	−11.394	21.895	−51.859	1	17.66	C
ATOM	960	C	HIS A	153	−12.829	21.891	−52.367	1	16.44	C
ATOM	961	O	HIS A	153	−13.682	22.586	−51.821	1	13.76	O
ATOM	962	CB	HIS A	153	−11.271	20.913	−50.69	1	13.32	C
ATOM	963	CG	HIS A	153	−10.048	21.124	−49.856	1	19.37	C
ATOM	964	ND1	HIS A	153	−8.865	20.454	−50.086	1	19.53	N
ATOM	965	CD2	HIS A	153	−9.819	21.941	−48.801	1	16.93	C
ATOM	966	CE1	HIS A	153	−7.963	20.843	−49.203	1	16.06	C
ATOM	967	NE2	HIS A	153	−8.516	21.746	−48.413	1	15.08	N
ATOM	968	H	HIS A	153	−11.565	23.68	−51.031	1	20.2	H
ATOM	969	HA	HIS A	153	−10.819	21.584	−52.576	1	21.19	H
ATOM	970	HB2	HIS A	153	−12.044	21.015	−50.113	1	15.98	H
ATOM	971	HB3	HIS A	153	−11.239	20.01	−51.041	1	15.98	H
ATOM	972	HD1	HIS A	153	−8.736	19.87	−50.705	1	23.43	H
ATOM	973	HD2	HIS A	153	−10.43	22.523	−48.411	1	20.31	H
ATOM	974	HE1	HIS A	153	−7.087	20.535	−49.149	1	19.27	H
ATOM	975	HE2	HIS A	153	8.124	22.146	−47.76	1	18.09	H
ATOM	976	N	TRP A	154	−13.094	21.106	−53.409	1	16.17	N
ATOM	977	CA	TRP A	154	−14.461	20.939	−53.897	1	16.21	C
ATOM	978	C	TRP A	154	−15.351	20.404	−52.787	1	14.86	C
ATOM	979	O	TRP A	154	−14.984	19.458	−52.093	1	13.34	O
ATOM	980	CB	TRP A	154	−14.523	19.976	−55.092	1	15.43	C
ATOM	981	CG	TRP A	154	−14.018	20.527	−56.39	1	17.31	C
ATOM	982	CD1	TRP A	154	−13.089	19.957	−57.21	1	18.38	C
ATOM	983	CD2	TRP A	154	−14.421	21.746	−57.029	1	22.3	C
ATOM	984	NE1	TRP A	154	−12.884	20.744	−58.317	1	20.02	N
ATOM	985	CE2	TRP A	154	−13.687	21.85	−58.23	1	22.6	C
ATOM	986	CE3	TRP A	154	−15.326	22.761	−56.702	1	18.3	C
ATOM	987	CZ2	TRP A	154	−13.831	22.927	−59.104	1	22.55	C
ATOM	988	CZ3	TRP A	154	−15.464	23.831	−57.568	1	19.05	C
ATOM	989	CH2	TRP A	154	−14.723	23.904	−58.757	1	23.4	C
ATOM	990	H	TRP A	154	−12.504	20.661	−53.848	1	19.4	H
ATOM	991	HA	TRP A	154	−14.808	21.799	−54.179	1	19.45	H
ATOM	992	HB2	TRP A	154	−13.992	19.192	−54.882	1	18.52	H
ATOM	993	HB3	TRP A	154	−15.447	19.714	−55.226	1	18.52	H
ATOM	994	HD1	TRP A	154	−12.657	19.15	−57.044	1	22.06	H
ATOM	995	HE1	TRP A	154	−12.338	20.572	−58.959	1	24.02	H
ATOM	996	HE3	TRP A	154	−15.821	22.72	−55.916	1	21.96	H
ATOM	997	HZ2	TRP A	154	−13.339	22.979	−59.891	1	27.07	H
ATOM	998	HZ3	TRP A	154	−16.064	24.511	−57.361	1	22.86	H
ATOM	999	HH2	TRP A	154	−14.838	24.635	−59.321	1	28.08	H
ATOM	1000	N	MET A	155	−16.514	21.022	−52.612	1	17.17	N
ATOM	1001	CA	MET A	155	−17.553	20.465	−51.758	1	15.84	C
ATOM	1002	C	MET A	155	−18.796	20.242	−52.615	1	16.3	C
ATOM	1003	O	MET A	155	−18.784	20.513	−53.816	1	19.47	O
ATOM	1004	CB	MET A	155	−17.852	21.382	−50.569	1	15.2	C
ATOM	1005	CG	MET A	155	−18.223	22.801	−50.94	1	12.06	C
ATOM	1006	SD	MET A	155	−18.683	23.761	−49.486	1	15.98	S
ATOM	1007	CE	MET A	155	−18.393	25.415	−50.109	1	15.7	C
ATOM	1008	H	MET A	155	−16.726	21.77	−52.98	1	20.6	H
ATOM	1009	HA	MET A	155	−17.252	19.612	−51.41	1	19.01	H
ATOM	1010	HB2	MET A	155	−18.592	21.006	−50.068	1	18.23	H
ATOM	1011	HB3	MET A	155	−17.064	21.423	−50.005	1	18.23	H
ATOM	1012	HG2	MET A	155	−17.463	23.231	−51.362	1	14.47	H
ATOM	1013	HG3	MET A	155	−18.98	22.785	−51.547	1	14.47	H
ATOM	1014	HE1	MET A	155	−18.606	26.056	−49.412	1	18.84	H
ATOM	1015	HE2	MET A	155	−17.461	25.498	−50.362	1	18.84	H
ATOM	1016	HE3	MET A	155	−18.961	25.565	−50.881	1	18.84	H
ATOM	1017	N	GLY A	156	−19.859	19.739	−52	1	16.55	N
ATOM	1018	CA	GLY A	156	−21.008	19.259	−52.744	1	17.95	C
ATOM	1019	C	GLY A	156	−22.078	20.285	−53.069	1	23.68	C
ATOM	1020	O	GLY A	156	−23.217	19.911	−53.339	1	23.71	O
ATOM	1021	H	GLY A	156	−19.937	19.667	−51.147	1	19.86	H
ATOM	1022	HA2	GLY A	156	−20.698	18.882	−53.582	1	21.54	H
ATOM	1023	HA3	GLY A	156	−21.428	18.546	−52.237	1	21.54	H
ATOM	1024	N	LEU A	157	−21.732	21.569	−53.048	1	20.6	N
ATOM	1025	CA	LEU A	157	−22.694	22.607	−53.407	1	26.74	C
ATOM	1026	C	LEU A	157	−22.917	22.621	−54.914	1	32.2	C
ATOM	1027	O	LEU A	157	−21.984	22.421	−55.695	1	30.5	O
ATOM	1028	CB	LEU A	157	−22.23	23.992	−52.945	1	23.22	C
ATOM	1029	CG	LEU A	157	−22.516	24.455	−51.512	1	27.17	C
ATOM	1030	CD1	LEU A	157	−22.148	25.924	−51.377	1	29.03	C
ATOM	1031	CD2	LEU A	157	−23.963	24.244	−51.093	1	26.6	C
ATOM	1032	H	LEU A	157	−20.953	21.864	−52.831	1	24.72	H
ATOM	1033	HA	LEU A	157	−23.543	22.415	−52.978	1	32.08	H
ATOM	1034	HB2	LEU A	157	−21.268	24.03	−53.059	1	27.87	H
ATOM	1035	HB3	LEU A	157	−22.639	24.647	−53.532	1	27.87	H
ATOM	1036	HG	LEU A	157	−21.954	23.951	−50.903	1	32.6	H
ATOM	1037	HD11	LEU A	157	−22.331	26.212	−50.469	1	34.83	H
ATOM	1038	HD12	LEU A	157	−21.205	26.033	−51.576	1	34.83	H
ATOM	1039	HD13	LEU A	157	−22.681	26.44	−52.002	1	34.83	H
ATOM	1040	HD21	LEU A	157	−24.076	24.556	−50.181	1	31.92	H
ATOM	1041	HD22	LEU A	157	−24.54	24.747	−51.689	1	31.92	H
ATOM	1042	HD23	LEU A	157	−24.173	23.299	−51.148	1	31.92	H
ATOM	1043	N	VAL A	158	−24.164	22.86	−55.306	1	35.94	N
ATOM	1044	CA	VAL A	158	−24.554	22.891	−56.709	1	35.15	C
ATOM	1045	C	VAL A	158	−25.361	24.154	−56.983	1	41.48	C
ATOM	1046	O	VAL A	158	−26.272	24.493	−56.226	1	36.73	O
ATOM	1047	CB	VAL A	158	−25.393	21.662	−57.097	1	38.21	C
ATOM	1048	CG1	VAL A	158	−25.423	21.504	−58.607	1	49.98	C
ATOM	1049	CG2	VAL A	158	−24.839	20.401	−56.443	1	39.33	C
ATOM	1050	H	VAL A	158	−24.816	23.011	−54.765	1	43.13	H
ATOM	1051	HA	VAL A	158	−23.759	22.908	−57.265	1	42.18	H
ATOM	1052	HB	VAL A	158	−26.303	21.787	−56.788	1	45.85	H
ATOM	1053	HG11	VAL A	158	−25.955	20.725	−58.832	1	59.98	H
ATOM	1054	HG12	VAL A	158	−25.816	22.299	−58.999	1	59.98	H
ATOM	1055	HG13	VAL A	158	−24.515	21.389	−58.93	1	59.98	H
ATOM	1056	HG21	VAL A	158	−25.386	19.644	−56.704	1	47.2	H
ATOM	1057	HG22	VAL A	158	−23.925	20.267	−56.739	1	47.2	H
ATOM	1058	HG23	VAL A	158	−24.863	20.51	−55.479	1	47.2	H
ATOM	1059	N	HIS A	159	−25.018	24.849	−58.062	1	40.87	N
ATOM	1060	CA	HIS A	159	−25.71	26.078	−58.427	1	49.33	C
ATOM	1061	C	HIS A	159	−26.895	25.782	−59.331	1	56.17	C
ATOM	1062	O	HIS A	159	−26.738	25.178	−60.39	1	50.22	O
ATOM	1063	CB	HIS A	159	−24.759	27.046	−59.131	1	49.48	C
ATOM	1064	CG	HIS A	159	−25.285	28.444	−59.229	1	56.01	C
ATOM	1065	ND1	HIS A	159	−24.876	29.324	−60.207	1	66.11	N
ATOM	1066	CD2	HIS A	159	−26.184	29.115	−58.47	1	57.64	C
ATOM	1067	CE1	HIS A	159	−25.502	30.477	−60.048	1	76.9	C
ATOM	1068	NE2	HIS A	159	−26.301	30.377	−59.001	1	68.99	N
ATOM	1069	H	HIS A	159	−24.386	24.629	−58.601	1	49.05	H
ATOM	1070	HA	HIS A	159	−26.041	26.509	−57.624	1	59.2	H
ATOM	1071	HB2	HIS A	159	−23.924	27.077	−58.639	1	59.38	H
ATOM	1072	HB3	HIS A	159	−24.598	26.726	−60.032	1	59.38	H
ATOM	1073	HD1	HIS A	159	−24.304	29.15	−60.825	1	79.33	H
ATOM	1074	HD2	HIS A	159	−26.637	28.784	−57.729	1	69.17	H
ATOM	1075	HE1	HIS A	159	−25.397	31.231	−60.582	1	92.28	H
ATOM	1076	HE2	HIS A	159	−26.811	31	−58.701	1	82.79	H
ATOM	1077	N	ILE A	160	−28.078	26.209	−58.904	1	63.42	N
ATOM	1078	CA	ILE A	160	−29.278	26.111	−59.725	1	74.82	C
ATOM	1079	C	ILE A	160	−29.379	27.349	−60.618	1	81.75	C
ATOM	1080	O	ILE A	160	−29.585	28.452	−60.113	1	78.84	O
ATOM	1081	CB	ILE A	160	−30.549	25.992	−58.859	1	74.4	C
ATOM	1082	CG1	ILE A	160	−30.45	24.786	−57.917	1	65.58	C
ATOM	1083	CG2	ILE A	160	−31.79	25.885	−59.736	1	81.67	C
ATOM	1084	CD1	ILE A	160	−30.357	23.442	−58.622	1	62.63	C
ATOM	1085	H	ILE A	160	−28.213	26.565	−58.132	1	76.11	H
ATOM	1086	HA	ILE A	160	−29.219	25.326	−60.292	1	89.78	H
ATOM	1087	HB	ILE A	160	−30.626	26.794	−58.319	1	89.28	H
ATOM	1088	HG12	ILE A	160	−29.657	24.886	−57.368	1	78.7	H
ATOM	1089	HG13	ILE A	160	−31.238	24.768	−57.352	1	78.7	H
ATOM	1090	HG21	ILE A	160	−32.573	25.811	−59.168	1	98	H
ATOM	1091	HG22	ILE A	160	−31.856	26.68	−60.288	1	98	H
ATOM	1092	HG23	ILE A	160	−31.713	25.097	−60.297	1	98	H
ATOM	1093	HD11	ILE A	160	−30.298	22.74	−57.955	1	75.15	H
ATOM	1094	HD12	ILE A	160	−31.15	23.316	−59.166	1	75.15	H
ATOM	1095	HD13	ILE A	160	−29.565	23.434	−59.182	1	75.15	H
ATOM	1096	N	PRO A	161	−29.227	27.178	−61.946	1	91.79	N
ATOM	1097	CA	PRO A	161	−29.299	28.358	−62.819	1	98.12	C
ATOM	1098	C	PRO A	161	−30.683	29.003	−62.824	1	100.1	C
ATOM	1099	O	PRO A	161	−30.811	30.182	−63.157	1	100.43	O
ATOM	1100	CB	PRO A	161	−28.959	27.797	−64.208	1	103.41	C
ATOM	1101	CG	PRO A	161	−28.314	26.477	−63.957	1	98.76	C
ATOM	1102	CD	PRO A	161	−28.948	25.953	−62.715	1	93.32	C
ATOM	1103	HA	PRO A	161	−28.634	29.015	−62.561	1	117.74	H
ATOM	1104	HB2	PRO A	161	−29.774	27.687	−64.723	1	124.09	H
ATOM	1105	HB3	PRO A	161	−28.346	28.398	−64.66	1	124.09	H
ATOM	1106	HG2	PRO A	161	−28.485	25.884	−64.705	1	118.52	H
ATOM	1107	HG3	PRO A	161	−27.36	26.6	−63.829	1	118.52	H
ATOM	1108	HD2	PRO A	161	−29.774	25.489	−62.925	1	111.99	H
ATOM	1109	HD3	PRO A	161	−28.33	25.383	−62.232	1	111.99	H
ATOM	1110	N	THR A	162	−31.699	28.227	−62.458	1	100.32	N
ATOM	1111	CA	THR A	162	−33.074	28.712	−62.425	1	102.58	C
ATOM	1112	C	THR A	162	−33.221	29.911	−61.488	1	98.89	C
ATOM	1113	O	THR A	162	−33.339	31.051	−61.94	1	100.64	O
ATOM	1114	CB	THR A	162	−34.048	27.597	−61.978	1	103.4	C
ATOM	1115	OG1	THR A	162	−33.897	26.454	−62.828	1	102.81	O
ATOM	1116	CG2	THR A	162	−35.492	28.078	−62.034	1	106.25	C
ATOM	1117	H	THR A	162	−31.616	27.405	−62.222	1	120.38	H
ATOM	1118	HA	THR A	162	−33.331	28.995	−63.316	1	123.09	H
ATOM	1119	HB	THR A	162	−33.847	27.345	−61.063	1	124.08	H
ATOM	1120	HG1	THR A	162	−34.066	26.664	−63.624	1	123.38	H
ATOM	1121	HG21	THR A	162	−36.089	27.368	−61.751	1	127.5	H
ATOM	1122	HG22	THR A	162	−35.61	28.842	−61.447	1	127.5	H
ATOM	1123	HG23	THR A	162	−35.719	28.339	−62.94	1	127.5	H
ATOM	1124	N	ASN A	163	−33.204	29.643	−60.185	1	94.97	N
ATOM	1125	CA	ASN A	163	−33.435	30.674	−59.178	1	91.11	C
ATOM	1126	C	ASN A	163	−32.14	31.232	−58.589	1	85.58	C
ATOM	1127	O	ASN A	163	−32.171	32.03	−57.651	1	80.37	O
ATOM	1128	CB	ASN A	163	−34.319	30.117	−58.057	1	85.28	C
ATOM	1129	CG	ASN A	163	−33.748	28.858	−57.431	1	81.5	C
ATOM	1130	OD1	ASN A	163	−32.899	28.188	−58.018	1	80.62	O
ATOM	1131	ND2	ASN A	163	−34.221	28.525	−56.236	1	76.73	N
ATOM	1132	H	ASN A	163	−33.06	28.862	−59.856	1	113.96	H
ATOM	1133	HA	ASN A	163	−33.912	31.411	−59.591	1	109.34	H
ATOM	1134	HB2	ASN A	163	−34.404	30.787	−57.36	1	102.34	H
ATOM	1135	HB3	ASN A	163	−35.192	29.903	−58.42	1	102.34	H
ATOM	1136	HD21	ASN A	163	−33.93	27.82	−55.839	1	92.07	H
ATOM	1137	HD22	ASN A	163	−34.819	29.015	−55.858	1	92.07	H
ATOM	1138	N	GLY A	164	−31.005	30.815	−59.141	1	84.69	N
ATOM	1139	CA	GLY A	164	−29.712	31.301	−58.69	1	79.34	C
ATOM	1140	C	GLY A	164	−29.381	30.898	−57.264	1	74.41	C
ATOM	1141	O	GLY A	164	−28.51	31.495	−56.63	1	68.03	O
ATOM	1142	H	GLY A	164	−30.959	30.245	−59.784	1	101.63	H
ATOM	1143	HA2	GLY A	164	−29.019	30.953	−59.273	1	95.2	H
ATOM	1144	HA3	GLY A	164	−29.698	32.269	−58.744	1	95.2	H
ATOM	1145	N	SER A	165	−30.073	29.88	−56.761	1	71.84	N
ATOM	1146	CA	SER A	165	−29.858	29.399	−55.402	1	60.5	C
ATOM	1147	C	SER A	165	−28.787	28.313	−55.373	1	53.12	C
ATOM	1148	O	SER A	165	−28.365	27.818	−56.418	1	52.63	O
ATOM	1149	CB	SER A	165	−31.163	28.861	−54.811	1	63.49	C
ATOM	1150	OG	SER A	165	−31.594	27.699	−55.498	1	66.5	O
ATOM	1151	H	SER A	165	−30.679	29.448	−57.192	1	86.21	H
ATOM	1152	HA	SER A	165	−29.556	30.135	−54.847	1	72.59	H
ATOM	1153	HB2	SER A	165	−31.018	28.639	−53.878	1	76.19	H
ATOM	1154	HB3	SER A	165	−31.848	29.544	−54.886	1	76.19	H
ATOM	1155	HG	SER A	165	−31.724	27.876	−56.309	1	79.8	H
ATOM	1156	N	TRP A	166	−28.355	27.956	−54.167	1	44.12	N
ATOM	1157	CA	TRP A	166	−27.377	26.893	−53.971	1	38.56	C
ATOM	1158	C	TRP A	166	−27.987	25.748	−53.173	1	36.68	C
ATOM	1159	O	TRP A	166	−28.722	25.969	−52.211	1	33.26	O
ATOM	1160	CB	TRP A	166	−26.135	27.424	−53.25	1	32.81	C
ATOM	1161	CG	TRP A	166	−25.29	28.347	−54.08	1	38.99	C
ATOM	1162	CD1	TRP A	166	−25.364	29.709	−54.125	1	41.82	C
ATOM	1163	CD2	TRP A	166	−24.237	27.973	−54.978	1	38.51	C
ATOM	1164	NE1	TRP A	166	−24.424	30.207	−54.996	1	39.58	N
ATOM	1165	CE2	TRP A	166	−23.72	29.162	−55.533	1	36.7	C
ATOM	1166	CE3	TRP A	166	−23.682	26.751	−55.366	1	35.41	C
ATOM	1167	CZ2	TRP A	166	−22.678	29.163	−56.458	1	35.25	C
ATOM	1168	CZ3	TRP A	166	−22.646	26.753	−56.282	1	32.08	C
ATOM	1169	CH2	TRP A	166	−22.154	27.952	−56.817	1	33.54	C
ATOM	1170	H	TRP A	166	−28.62	28.321	−53.435	1	52.94	H
ATOM	1171	HA	TRP A	166	−27.102	26.548	−54.835	1	46.28	H
ATOM	1172	HB2	TRP A	166	−26.418	27.912	−52.461	1	39.37	H
ATOM	1173	HB3	TRP A	166	−25.581	26.672	−52.989	1	39.37	H
ATOM	1174	HD1	TRP A	166	−25.964	30.226	−53.637	1	50.18	H
ATOM	1175	HE1	TRP A	166	−24.3	31.039	−55.177	1	47.49	H
ATOM	1176	HE3	TRP A	166	−24.003	25.951	−55.015	1	42.49	H
ATOM	1177	HZ2	TRP A	166	−22.348	29.956	−56.813	1	42.3	H
ATOM	1178	HZ3	TRP A	166	−22.27	25.946	−56.548	1	38.5	H
ATOM	1179	HH2	TRP A	166	−21.457	27.923	−57.432	1	40.24	H
ATOM	1180	N	GLN A	167	−27.678	24.524	−53.583	1	31.8	N
ATOM	1181	CA	GLN A	167	−28.116	23.343	−52.859	1	37.87	C
ATOM	1182	C	GLN A	167	−27.035	22.268	−52.901	1	26.79	C
ATOM	1183	0	GLN A	167	−26.107	22.337	−53.706	1	25.74	O
ATOM	1184	CB	GLN A	167	−29.425	22.807	−53.444	1	40.72	C
ATOM	1185	CG	GLN A	167	−29.394	22.6	−54.947	1	46.08	C
ATOM	1186	CD	GLN A	167	−30.494	21.674	−55.428	1	45.1	C
ATOM	1187	OE1	GLN A	167	−30.226	20.635	−56.033	1	47.82	O
ATOM	1188	NE2	GLN A	167	−31.737	22.046	−55.162	1	41.89	N
ATOM	1189	H	GLN A	167	−27.212	24.352	−54.285	1	38.17	H
ATOM	1190	HA	GLN A	167	−28.273	23.578	−51.932	1	45.44	H
ATOM	1191	HB2	GLN A	167	−29.623	21.952	−53.032	1	48.87	H
ATOM	1192	HB3	GLN A	167	−30.135	23.438	−53.248	1	48.87	H
ATOM	1193	HG2	GLN A	167	−29.507	23.457	−55.387	1	55.29	H
ATOM	1194	HG3	GLN A	167	−28.541	22.209	−55.195	1	55.29	H
ATOM	1195	HE21	GLN A	167	−32.397	21.555	−55.414	1	50.26	H
ATOM	1196	HE22	GLN A	167	−31.885	22.779	−54.737	1	50.26	H
ATOM	1197	N	TRP A	168	−27.159	21.284	−52.019	1	29	N
ATOM	1198	CA	TRP A	168	−26.234	20.16	−51.988	1	25.2	C
ATOM	1199	C	TRP A	168	−26.642	19.126	−53.024	1	33.37	C
ATOM	1200	O	TRP A	168	−27.778	19.137	−53.5	1	26.7	O
ATOM	1201	CB	TRP A	168	−26.194	19.554	−50.59	1	25.54	C
ATOM	1202	CG	TRP A	168	−25.774	20.563	−49.587	1	26.46	C
ATOM	1203	CD1	TRP A	168	−26.564	21.196	−48.677	1	29.23	C
ATOM	1204	CD2	TRP A	168	−24.458	21.094	−49.417	1	24.51	C
ATOM	1205	NE1	TRP A	168	−25.818	22.082	−47.938	1	25.79	N
ATOM	1206	CE2	TRP A	168	−24.52	22.038	−48.376	1	20.96	C
ATOM	1207	CE3	TRP A	168	−23.231	20.858	−50.044	1	20.74	C
ATOM	1208	CZ2	TRP A	168	−23.402	22.746	−47.944	1	18.61	C
ATOM	1209	CZ3	TRP A	168	−22.122	21.558	−49.613	1	18.82	C
ATOM	1210	CH2	TRP A	168	−22.215	22.493	−48.573	1	19.65	C
ATOM	1211	H	TRP A	168	−27.777	21.244	−51.423	1	34.8	H
ATOM	1212	HA	TRP A	168	−25.343	20.474	−52.207	1	30.24	H
ATOM	1213	HB2	TRP A	168	−27.078	19.235	−50.351	1	30.65	H
ATOM	1214	HB3	TRP A	168	−25.556	18.823	−50.573	1	30.65	H
ATOM	1215	HD1	TRP A	168	−27.476	21.048	−48.569	1	35.07	H
ATOM	1216	HE1	TRP A	168	−26.116	22.582	−47.306	1	30.95	H
ATOM	1217	HE3	TRP A	168	−23.162	20.241	−50.736	1	24.89	H
ATOM	1218	HZ2	TRP A	168	−23.459	23.364	−47.251	1	22.33	H
ATOM	1219	HZ3	TRP A	168	−21.3	21.41	−50.023	1	22.59	H
ATOM	1220	HH2	TRP A	168	−21.451	22.949	−48.303	1	23.58	H
ATOM	1221	N	GLU A	169	−25.718	18.238	−53.379	1	30.13	N
ATOM	1222	CA	GLU A	169	−25.959	17.297	−54.468	1	31.2	C
ATOM	1223	C	GLU A	169	−27.056	16.293	−54.122	1	30.15	C
ATOM	1224	O	GLU A	169	−27.646	15.685	−55.013	1	35.52	O
ATOM	1225	CB	GLU A	169	−24.668	16.564	−54.842	1	34.22	C
ATOM	1226	CG	GLU A	169	−24.055	15.756	−53.726	1	30.07	C
ATOM	1227	CD	GLU A	169	−22.585	15.446	−53.98	1	32.91	C
ATOM	1228	OE1	GLU A	169	−22.224	15.153	−55.14	1	30.13	O
ATOM	1229	OE2	GLU A	169	−21.789	15.504	−53.021	1	27.4	O1−
ATOM	1230	H	GLU A	169	−24.947	18.16	−53.007	1	36.15	H
ATOM	1231	HA	GLU A	169	−26.252	17.794	−55.248	1	37.44	H
ATOM	1232	HB2	GLU A	169	−24.858	15.957	−55.574	1	41.07	H
ATOM	1233	HB3	GLU A	169	−24.011	17.219	−55.125	1	41.07	H
ATOM	1234	HG2	GLU A	169	−24.119	16.257	−52.898	1	36.08	H
ATOM	1235	HG3	GLU A	169	−24.531	14.914	−53.644	1	36.08	H
ATOM	1236	N	ASP A	170	−27.342	16.132	−52.834	1	31.34	N
ATOM	1237	CA	ASP A	170	−28.442	15.27	−52.412	1	30.16	C
ATOM	1238	C	ASP A	170	−29.781	15.998	−52.539	1	31.43	C
ATOM	1239	O	ASP A	170	−30.818	15.485	−52.124	1	29.59	O
ATOM	1240	CB	ASP A	170	−28.229	14.785	−50.974	1	32.21	C
ATOM	1241	CG	ASP A	170	−28.404	15.887	−49.939	1	31.98	C
ATOM	1242	OD1	ASP A	170	−28.531	17.071	−50.314	1	33.58	O
ATOM	1243	OD2	ASP A	170	−28.398	15.562	−48.733	1	27.25	O1−
ATOM	1244	H	ASP A	170	−26.918	16.508	−52.187	1	37.61	H
ATOM	1245	HA	ASP A	170	−28.47	14.491	−52.989	1	36.19	H
ATOM	1246	HB2	ASP A	170	−28.874	14.087	−50.779	1	38.65	H
ATOM	1247	HB3	ASP A	170	−27.328	14.435	−50.89	1	38.65	H
ATOM	1248	N	GLY A	171	−29.741	17.204	−53.098	1	35.35	N
ATOM	1249	CA	GLY A	171	−30.939	17.987	−53.336	1	37.34	C
ATOM	1250	C	GLY A	171	−31.329	18.85	−52.152	1	34.83	C
ATOM	1251	O	GLY A	171	−32.126	19.779	−52.294	1	36.63	O
ATOM	1252	H	GLY A	171	−29.017	17.594	−53.351	1	42.42	H
ATOM	1253	HA2	GLY A	171	−30.798	18.565	−54.102	1	44.81	H
ATOM	1254	HA3	GLY A	171	−31.678	17.39	−53.535	1	44.81	H
ATOM	1255	N	SER A	172	−30.76	18.555	−50.987	1	33.06	N
ATOM	1256	CA	SER A	172	−31.137	19.238	−49.752	1	34.83	C
ATOM	1257	C	SER A	172	−30.789	20.72	−49.789	1	39	C
ATOM	1258	O	SER A	172	−30.003	21.17	−50.623	1	36.04	O
ATOM	1259	CB	SER A	172	−30.454	18.589	−48.551	1	37.68	C
ATOM	1260	OG	SER A	172	−29.067	18.869	−48.56	1	31.69	O
ATOM	1261	H	SER A	172	−30.149	17.959	−50.883	1	39.68	H
ATOM	1262	HA	SER A	172	−32.096	19.16	−49.63	1	41.8	H
ATOM	1263	HB2	SER A	172	−30.844	18.943	−47.736	1	45.22	H
ATOM	1264	HB3	SER A	172	−30.584	17.629	−48.593	1	45.22	H
ATOM	1265	HG	SER A	172	−28.718	18.569	−49.263	1	38.03	H
ATOM	1266	N	ILE A	173	−31.374	21.467	−48.859	1	40.76	N
ATOM	1267	CA	ILE A	173	−31.214	22.915	−48.809	1	44.21	C
ATOM	1268	C	ILE A	173	−29.943	23.328	−48.07	1	35.14	C
ATOM	1269	O	ILE A	173	−29.563	22.716	−47.069	1	35.11	O
ATOM	1270	CB	ILE A	173	−32.431	23.587	−48.128	1	50.72	C
ATOM	1271	CG1	ILE A	173	−32.642	23.026	−46.711	1	49.11	C
ATOM	1272	CG2	ILE A	173	−33.678	23.388	−48.982	1	62.02	C
ATOM	1273	CD1	ILE A	173	−33.764	23.689	−45.932	1	53.43	C
ATOM	1274	H	ILE A	173	−31.876	21.153	−48.236	1	48.91	H
ATOM	1275	HA	ILE A	173	−31.154	23.254	−49.716	1	53.05	H
ATOM	1276	HB	ILE A	173	−32.256	24.538	−48.058	1	60.86	H
ATOM	1277	HG12	ILE A	173	−32.849	22.081	−46.779	1	58.93	H
ATOM	1278	HG13	ILE A	173	−31.822	23.145	−46.205	1	58.93	H
ATOM	1279	HG21	ILE A	173	−34.431	23.814	−48.543	1	74.42	H
ATOM	1280	HG22	ILE A	173	−33.532	23.79	−49.852	1	74.42	H
ATOM	1281	HG23	ILE A	173	−33.845	22.438	−49.079	1	74.42	H
ATOM	1282	HD11	ILE A	173	−33.826	23.276	−45.056	1	64.11	H
ATOM	1283	HD12	ILE A	173	−33.568	24.634	−45.84	1	64.11	H
ATOM	1284	HD13	ILE A	173	−34.596	23.568	−46.415	1	64.11	H
ATOM	1285	N	LEU A	174	−29.284	24.363	−48.579	1	36.19	N
ATOM	1286	CA	LEU A	174	−28.194	25.002	−47.854	1	33.01	C
ATOM	1287	C	LEU A	174	−28.785	25.874	−46.762	1	25.23	C
ATOM	1288	O	LEU A	174	−29.378	26.91	−47.051	1	35.07	O
ATOM	1289	CB	LEU A	174	−27.317	25.839	−48.788	1	28.79	C
ATOM	1290	CG	LEU A	174	−26.268	26.722	−48.096	1	30.47	C
ATOM	1291	CD1	LEU A	174	−25.235	25.873	−47.369	1	28.59	C
ATOM	1292	CD2	LEU A	174	−25.593	27.65	−49.086	1	23.68	C
ATOM	1293	H	LEU A	174	−29.449	24.715	−49.346	1	43.42	H
ATOM	1294	HA	LEU A		174	−27.64	24.322	−47.438	1	39.62	H
ATOM	1295	HB2	LEU A	174	−26.843	25.238	−49.385	1	34.54	H
ATOM	1296	HB3	LEU A	174	−27.892	26.422	−49.307	1	34.54	H
ATOM	1297	HG	LEU A		174	−26.715	27.273	−47.434	1	36.57	H
ATOM	1298	HD11	LEU A	174	−24.589	26.458	−46.944	1	34.31	H
ATOM	1299	HD12	LEU A	174	−25.685	25.334	−46.699	1	34.31	H
ATOM	1300	HD13	LEU A	174	−24.79	25.299	−48.012	1	34.31	H
ATOM	1301	HD21	LEU A	174	−24.939	28.191	−48.616	1	28.42	H
ATOM	1302	HD22	LEU A	174	−25.154	27.119	−49.768	1	28.42	H
ATOM	1303	HD23	LEU A	174	−26.265	28.221	−49.492	1	28.42	H
ATOM	1304	N	SER A	175	−28.63	25.45	−45.513	1	30.51	N
ATOM	1305	CA	SER A	175	−29.152	26.205	−44.382	1	30.76	C
ATOM	1306	C	SER A	175	−28.581	27.619	−44.38	1	30.6	C
ATOM	1307	O	SER A	175	−27.416	27.82	−44.727	1	29.98	O
ATOM	1308	CB	SER A	175	−28.819	25.511	−43.063	1	29.16	C
ATOM	1309	OG	SER A	175	−29.013	24.111	−43.155	1	41.38	O
ATOM	1310	H	SER A	175	−28.224	24.724	−45.293	1	36.61	H
ATOM	1311	HA	SER A	175	−30.117	26.267	−44.458	1	36.91	H
ATOM	1312	HB2	SER A	175	−27.891	25.686	−42.842	1	35	H
ATOM	1313	HB3	SER A	175	−29.396	25.863	−42.368	1	35	H
ATOM	1314	HG	SER A	175	−28.825	23.746	−42.422	1	49.66	H
ATOM	1315	N	PRO A	176	−29.399	28.608	−43.989	1	27.59	N
ATOM	1316	CA	PRO A	176	−28.904	29.986	−43.961	1	27.04	C
ATOM	1317	C	PRO A	176	−27.802	30.194	−42.923	1	27.52	C
ATOM	1318	O	PRO A	176	−27.783	29.514	−41.898	1	28.41	O
ATOM	1319	CB	PRO A	176	−30.154	30.8	−43.603	1	27.57	C
ATOM	1320	CG	PRO A	176	−31.03	29.849	−42.883	1	31.89	C
ATOM	1321	CD	PRO A	176	−30.791	28.51	−43.515	1	24.67	C
ATOM	1322	HA	PRO A	176	−28.583	30.252	−44.837	1	32.45	H
ATOM	1323	HB2	PRO A	176	−29.908	31.544	−43.03	1	33.08	H
ATOM	1324	HB3	PRO A	176	−30.583	31.117	−44.414	1	33.08	H
ATOM	1325	HG2	PRO A	176	−30.787	29.831	−41.944	1	38.27	H
ATOM	1326	HG3	PRO A	176	−31.957	30.116	−42.99	1	38.27	H
ATOM	1327	HD2	PRO A	176	−30.876	27.804	−42.856	1	29.6	H
ATOM	1328	HD3	PRO A	176	−31.394	28.376	−44.262	1	29.6	H
ATOM	1329	N	ASN A	177	−26.89	31.117	−43.213	1	26.69	N
ATOM	1330	CA	ASN A	177	−25.849	31.524	−42.273	1	28.9	C
ATOM	1331	C	ASN A	177	−24.926	30.384	−41.861	1	30.53	C
ATOM	1332	O	ASN A	177	−24.475	30.324	−40.719	1	37.62	O
ATOM	1333	CB	ASN A	177	−26.488	32.149	−41.034	1	32.1	C
ATOM	1334	CG	ASN A	177	−27.336	33.353	−41.374	1	27.74	C
ATOM	1335	OD1	ASN A	177	−26.88	34.275	−42.05	1	29.89	O
ATOM	1336	ND2	ASN A	177	−28.585	33.345	−40.927	1	27.4	N
ATOM	1337	H	ASN A	177	−26.853	31.532	−43.965	1	32.03	H
ATOM	1338	HA	ASN A	177	−25.302	32.204	−42.696	1	34.68	H
ATOM	1339	HB2	ASN A	177	−27.057	31.492	−40.604	1	38.52	H
ATOM	1340	HB3	ASN A	177	−25.789	32.435	−40.426	1	38.52	H
ATOM	1341	HD21	ASN A	177	−29.106	34.008	−41.095	1	32.88	H
ATOM	1342	HD22	ASN A	177	−28.873	32.676	−40.469	1	32.88	H
ATOM	1343	N	LEU A	178	−24.646	29.488	−42.802	1	23.55	N
ATOM	1344	CA	LEU A	178	−23.682	28.417	−42.587	1	26.07	C
ATOM	1345	C	LEU A	178	−22.392	28.718	−43.335	1	25.37	C
ATOM	1346	O	LEU A	178	−21.299	28.646	−42.771	1	26.43	O
ATOM	1347	CB	LEU A	178	−24.243	27.071	−43.052	1	27.18	C
ATOM	1348	CG	LEU A	178	−24.863	26.136	−42.012	1	31.75	C
ATOM	1349	CD1	LEU A	178	−25.286	24.847	−42.694	1	32.44	C
ATOM	1350	CD2	LEU A	178	−23.906	25.83	−40.869	1	27.31	C
ATOM	1351	H	LEU A	178	−25.006	29.479	−43.583	1	28.26	H
ATOM	1352	HA	LEU A	178	−23.478	28.353	−41.641	1	31.28	H
ATOM	1353	HB2	LEU A	178	−24.931	27.249	−43.712	1	32.62	H
ATOM	1354	HB3	LEU A	178	−23.522	26.579	−43.475	1	32.62	H
ATOM	1355	HG	LEU A	178	−25.655	26.555	−41.639	1	38.1	H
ATOM	1356	HD11	LEU A	178	−25.679	24.255	−42.034	1	38.93	H
ATOM	1357	HD12	LEU A	178	−25.937	25.054	−43.383	1	38.93	H
ATOM	1358	HD13	LEU A	178	−24.505	24.43	−43.091	1	38.93	H
ATOM	1359	HD21	LEU A	178	−24.345	25.236	−40.24	1	32.77	H
ATOM	1360	HD22	LEU A	178	−23.113	25.403	−41.228	1	32.77	H
ATOM	1361	HD23	LEU A	178	−23.665	26.66	−40.428	1	32.77	H
ATOM	1362	N	LEU A	179	−22.536	29.044	−44.614	1	21.47	N
ATOM	1363	CA	LEU A	179	−21.403	29.358	−45.471	1	22.73	C
ATOM	1364	C	LEU A		179	−21.496	30.785	−45.977	1	24.99	C
ATOM	1365	O	LEU A	179	−22.58	31.279	−46.292	1	21.88	O
ATOM	1366	CB	LEU A	179	−21.34	28.399	−46.66	1	20.75	C
ATOM	1367	CG	LEU A		179	−21.094	26.923	−46.352	1	20.55	C
ATOM	1368	CD1	LEU A		179	−21.138	26.111	−47.637	1	23.59	C
ATOM	1369	CD2	LEU A		179	−19.764	26.739	−45.65	1	20.81	C
ATOM	1370	H	LEU A	179	−23.295	29.09	−45.015	1	25.76	H
ATOM	1371	HA	LEU A	179	−20.582	29.267	−44.963	1	27.27	H
ATOM	1372	HB2	LEU A	179	−22.182	28.454	−47.137	1	24.9	H
ATOM	1373	HB3	LEU A	179	−20.623	28.691	−47.245	1	24.9	H
ATOM	1374	HG	LEU A	179	−21.795	26.598	−45.764	1	24.66	H
ATOM	1375	HD11	LEU A	179	−20.98	25.178	−47.426	1	28.3	H
ATOM	1376	HD12	LEU A		179	−22.011	26.216	−48.047	1	28.3	H
ATOM	1377	HD13	LEU A	179	−20.449	26.436	−48.238	1	28.3	H
ATOM	1378	HD21	LEU A	179	−19.632	25.796	−45.465	1	24.97	H
ATOM	1379	HD22	LEU A		179	−19.055	27.066	−46.226	1	24.97	H
ATOM	1380	HD23	LEU A	179	−19.773	27.241	−44.82	1	24.97	H
ATOM	1381	N	THR A	180	−20.347	31.443	−46.038	1	21.26	N
ATOM	1382	CA	THR A	180	−20.231	32.721	−46.711	1	19.84	C
ATOM	1383	C	THR A	180	−19.779	32.441	−48.136	1	21.52	C
ATOM	1384	O	THR A	180	−18.64	32.036	−48.366	1	23.27	O
ATOM	1385	CB	THR A	180	−19.238	33.651	−45.993	1	24.67	C
ATOM	1386	OG1	THR A	180	−19.714	33.921	−44.669	1	25.74	O
ATOM	1387	CG2	THR A	180	−19.074	34.963	−46.744	1	25.66	C
ATOM	1388	H	THR A	180	−19.612	31.164	−45.691	1	25.51	H
ATOM	1389	HA	THR A	180	−21.098	33.155	−46.74	1	23.81	H
ATOM	1390	HB	THR A	180	−18.372	33.218	−45.942	1	29.61	H
ATOM	1391	HG1	THR A	180	−19.784	33.203	−44.237	1	30.89	H
ATOM	1392	HG21	THR A	180	−18.445	35.535	−46.276	1	30.8	H
ATOM	1393	HG22	THR A	180	−18.741	34.793	−47.639	1	30.8	H
ATOM	1394	HG23	THR A	180	−19.928	35.418	−46.806	1	30.8	H
ATOM	1395	N	ILE A	181	−20.683	32.633	−49.089	1	22.03	N
ATOM	1396	CA	ILE A	181	−20.372	32.385	−50.49	1	21.98	C
ATOM	1397	C	ILE A	181	−19.733	33.621	−51.1	1	25.54	C
ATOM	1398	O	ILE A	181	−20.283	34.72	−51.025	1	23.45	O
ATOM	1399	CB	ILE A	181	−21.623	31.998	−51.297	1	25.31	C
ATOM	1400	CG1	ILE A	181	−22.295	30.767	−50.684	1	27.58	C
ATOM	1401	CG2	ILE A	181	−21.257	31.731	−52.759	1	29.37	C
ATOM	1402	CD1	ILE A	181	−21.409	29.523	−50.619	1	25.67	C
ATOM	1403	H	ILE A	181	−21.487	32.906	−48.95	1	26.43	H
ATOM	1404	HA	ILE A	181	−19.736	31.655	−50.55	1	26.37	H
ATOM	1405	HB	ILE A	181	−22.249	32.738	−51.267	1	30.37	H
ATOM	1406	HG12	ILE A	181	−22.567	30.982	−49.778	1	33.09	H
ATOM	1407	HG13	ILE A	181	−23.076	30.544	−51.215	1	33.09	H
ATOM	1408	HG21	ILE A	181	−22.061	31.489	−53.246	1	35.24	H
ATOM	1409	HG22	ILE A	181	−20.869	32.534	−53.139	1	35.24	H
ATOM	1410	HG23	ILE A	181	−20.617	31.003	−52.796	1	35.24	H
ATOM	1411	HD11	ILE A	181	−21.913	28.797	−50.219	1	30.81	H
ATOM	1412	HD12	ILE A	181	−21.138	29.282	−51.519	1	30.81	H
ATOM	1413	HD13	ILE A	181	−20.628	29.72	−50.079	1	30.81	H
ATOM	1414	N	ILE A	182	−18.567	33.418	−51.706	1	21.72	N
ATOM	1415	CA	ILE A	182	−17.765	34.497	−52.261	1	20.53	C
ATOM	1416	C	ILE A	182	−17.654	34.34	−53.767	1	23.4	C
ATOM	1417	O	ILE A	182	−17.226	33.296	−54.256	1	22.37	O
ATOM	1418	CB	ILE A	182	−16.346	34.515	−51.649	1	20.38	C
ATOM	1419	CG1	ILE A	182	−16.43	34.684	−50.132	1	20.79	C
ATOM	1420	CG2	ILE A	182	−15.494	35.626	−52.271	1	21.86	C
ATOM	1421	CD1	ILE A	182	−15.132	34.434	−49.414	1	22.03	C
ATOM	1422	H	ILE A	182	−18.211	32.641	−51.808	1	26.06	H
ATOM	1423	HA	ILE A	182	−18.192	35.347	−52.072	1	24.63	H
ATOM	1424	HB	ILE A	182	−15.922	33.664	−51.838	1	24.45	H
ATOM	1425	HG12	ILE A	182	−16.706	35.593	−49.934	1	24.95	H
ATOM	1426	HG13	ILE A	182	−17.085	34.059	−49.784	1	24.95	H
ATOM	1427	HG21	ILE A	182	−14.613	35.611	−51.867	1	26.24	H
ATOM	1428	HG22	ILE A	182	−15.424	35.472	−53.226	1	26.24	H
ATOM	1429	HG23	ILE A	182	−15.921	36.481	−52.104	1	26.24	H
ATOM	1430	HD11	ILE A	182	−15.269	34.561	−48.462	1	26.43	H
ATOM	1431	HD12	ILE A	182	−14.845	33.524	−49.589	1	26.43	H
ATOM	1432	HD13	ILE A	182	−14.466	35.06	−49.74	1	26.43	H
ATOM	1433	N	GLU A	183	−18.035	35.379	−54.5	1	21.68	N
ATOM	1434	CA	GLU A	183	−17.855	35.391	−55.943	1	27.56	C
ATOM	1435	C	GLU A	183	−16.373	35.527	−56.271	1	29.48	C
ATOM	1436	O	GLU A	183	−15.667	36.337	−55.67	1	31.01	O
ATOM	1437	CB	GLU A	183	−18.648	36.533	−56.582	1	39.38	C
ATOM	1438	CG	GLU A	183	−20.154	36.416	−56.407	1	45.85	C
ATOM	1439	CD	GLU A	183	−20.911	37.55	−57.074	1	71.49	C
ATOM	1440	OE1	GLU A	183	−20.297	38.607	−57.336	1	65.31	O
ATOM	1441	OE2	GLU A	183	−22.12	37.382	−57.34	1	84.35	O1−
ATOM	1442	H	GLU A	183	−18.402	36.09	−54.184	1	26.02	H
ATOM	1443	HA	GLU A	183	−18.174	34.553	−56.314	1	33.07	H
ATOM	1444	HB2	GLU A	183	−18.368	37.37	−56.18	1	47.25	H
ATOM	1445	HB3	GLU A	183	−18.461	36.548	−57.534	1	47.25	H
ATOM	1446	HG2	GLU A	183	−20.454	35.582	−56.802	1	55.02	H
ATOM	1447	HG3	GLU A	183	−20.364	36.43	−55.461	1	55.02	H
ATOM	1448	N	MET A	184	−15.908	34.723	−57.219	1	27.36	N
ATOM	1449	CA	MET A	184	−14.52	34.765	−57.655	1	30.39	C
ATOM	1450	C	MET A	184	−14.461	34.514	−59.154	1	36.58	C
ATOM	1451	O	MET A	184	−14.269	35.441	−59.942	1	34.99	O
ATOM	1452	CB	MET A	184	−13.684	33.732	−56.895	1	28.2	C
ATOM	1453	CG	MET A	184	−12.2	33.78	−57.213	1	26.4	C
ATOM	1454	SD	MET A	184	−11.3	32.412	−56.469	1	27.32	S
ATOM	1455	CE	MET A	184	−11.827	31.057	−57.524	1	31.27	C
ATOM	1456	H	MET A	184	−16.384	34.136	−57.631	1	32.83	H
ATOM	1457	HA	MET A	184	−14.155	35.644	−57.466	1	36.47	H
ATOM	1458	HB2	MET A	184	−13.788	33.887	−55.943	1	33.85	H
ATOM	1459	HB3	MET A	184	−14.006	32.845	−57.12	1	33.85	H
ATOM	1460	HG2	MET A	184	−12.08	33.732	−58.175	1	31.68	H
ATOM	1461	HG3	MET A	184	−11.828	34.607	−56.871	1	31.68	H
ATOM	1462	HE1	MET A	184	−11.402	30.239	−57.223	1	37.53	H
ATOM	1463	HE2	MET A	184	−12.791	30.969	−57.468	1	37.53	H
ATOM	1464	HE3	MET A	184	−11.565	31.248	−58.439	1	37.53	H
ATOM	1465	N	GLN A	185	−14.639	33.253	−59.535	1	34.02	N
ATOM	1466	CA	GLN A	185	−14.708	32.865	−60.935	1	39.99	C
ATOM	1467	C	GLN A	185	−16.136	32.439	−61.257	1	36.81	C
ATOM	1468	O	GLN A	185	−16.749	31.687	−60.498	1	32.57	O
ATOM	1469	CB	GLN A	185	−13.724	31.732	−61.23	1	31.78	C
ATOM	1470	CG	GLN A	185	−13.525	31.454	−62.708	1	37.09	C
ATOM	1471	CD	GLN A	185	−12.853	32.606	−63.427	1	49.35	C
ATOM	1472	OE1	GLN A	185	−11.834	33.129	−62.972	1	44.78	O
ATOM	1473	NE2	GLN A	185	−13.427	33.014	−64.554	1	50.69	N
ATOM	1474	H	GLN A	185	−14.723	32.593	−58.99	1	40.83	H
ATOM	1475	HA	GLN A	185	−14.48	33.624	−61.494	1	47.99	H
ATOM	1476	HB2	GLN A	185	−12.86	31.964	−60.855	1	38.14	H
ATOM	1477	HB3	GLN A	185	−14.053	30.918	−60.818	1	38.14	H
ATOM	1478	HG2	GLN A	185	−12.966	30.668	−62.81	1	44.51	H
ATOM	1479	HG3	GLN A	185	−14.39	31.304	−63.121	1	44.51	H
ATOM	1480	HE21	GLN A	185	−13.084	33.665	−64.999	1	60.83	H
ATOM	1481	HE22	GLN A	185	−14.141	32.629	−64.837	1	60.83	H
ATOM	1482	N	LYS A	186	−16.669	32.933	−62.37	1	41.91	N
ATOM	1483	CA	LYS A	186	−18.026	32.585	−62.779	1	44.77	C
ATOM	1484	C	LYS A	186	−18.149	31.085	−63.028	1	32.82	C
ATOM	1485	O	LYS A	186	−17.492	30.537	−63.913	1	41.23	O
ATOM	1486	CB	LYS A	186	−18.427	33.361	−64.033	1	55.29	C
ATOM	1487	CG	LYS A	186	−18.429	34.868	−63.851	1	69.71	C
ATOM	1488	CD	LYS A	186	−18.935	35.578	−65.096	1	87.98	C
ATOM	1489	CE	LYS A	186	−18.822	37.087	−64.961	1	90.78	C
ATOM	1490	NZ	LYS A	186	−17.407	37.529	−64.823	1	89.35	N1+
ATOM	1491	H	LYS A	186	−16.266	33.47	−62.907	1	50.3	H
ATOM	1492	HA	LYS A		186	−18.642	32.823	−62.068	1	53.72	H
ATOM	1493	HB2	LYS A	186	−17.802	33.15	−64.744	1	66.35	H
ATOM	1494	HB3	LYS A	186	−19.323	33.093	−64.293	1	66.35	H
ATOM	1495	HG2	LYS A	186	−19.012	35.1	−63.11	1	83.65	H
ATOM	1496	HG3	LYS A	186	−17.525	35.171	−63.674	1	83.65	H
ATOM	1497	HD2	LYS A	186	−18.406	35.301	−65.86	1	105.57	H
ATOM	1498	HD3	LYS A	186	−19.869	35.354	−65.235	1	105.57	H
ATOM	1499	HE2	LYS A		186	−19.194	37.507	−65.753	1	108.94	H
ATOM	1500	HE3	LYS A	186	−19.307	37.374	−64.172	1	108.94	H
ATOM	1501	HZ1	LYS A	186	−16.94	37.281	−65.54	1	107.22	H
ATOM	1502	HZ2	LYS A		186	−17.371	38.415	−64.747	1	107.22	H
ATOM	1503	HZ3	LYS A		186	−17.043	37.16	−64.1	1	107.22	H
ATOM	1504	N	GLY A	187	−18.991	30.427	−62.239	1	31.79	N
ATOM	1505	CA	GLY A	187	−19.178	28.993	−62.35	1	33.62	C
ATOM	1506	C	GLY A	187	−20.338	28.512	−61.506	1	28.83	C
ATOM	1507	O	GLY A	187	−20.967	29.303	−60.803	1	31.67	O
ATOM	1508	H	GLY A	187	−19.468	30.795	−61.626	1	38.15	H
ATOM	1509	HA2	GLY A	187	−19.35	28.758	−63.276	1	40.35	H
ATOM	1510	HA3	GLY A	187	−18.373	28.536	−62.06	1	40.35	H
ATOM	1511	N	ASP A	188	−20.613	27.211	−61.571	1	26.78	N
ATOM	1512	CA	ASP A	188	−21.741	26.613	−60.86	1	29.71	C
ATOM	1513	C	ASP A	188	−21.302	25.691	−59.721	1	27.78	C
ATOM	1514	O	ASP A	188	−22.11	24.929	−59.185	1	26.36	O
ATOM	1515	CB	ASP A	188	−22.617	25.84	−61.843	1	34.87	C
ATOM	1516	CG	ASP A	188	−23.227	26.735	−62.901	1	39.7	C
ATOM	1517	OD1	ASP A	188	−23.676	27.848	−62.551	1	38.4	O
ATOM	1518	OD2	ASP A	188	−23.248	26.332	−64.083	1	40.4	O1−
ATOM	1519	H	ASP A	188	−20.154	26.645	−62.028	1	32.14	H
ATOM	1520	HA	ASP A	188	−22.28	27.322	−60.476	1	35.65	H
ATOM	1521	HB2	ASP A	188	−22.077	25.17	−62.291	1	41.85	H
ATOM	1522	HB3	ASP A	188	−23.34	25.413	−61.357	1	41.85	H
ATOM	1523	N	CYS A	189	−20.027	25.772	−59.349	1	25.17	N
ATOM	1524	CA	CYS A	189	−19.485	24.978	−58.248	1	21.3	C
ATOM	1525	C	CYS A	189	−18.739	25.877	−57.264	1	22.52	C
ATOM	1526	O	CYS A	189	−18.363	27.001	−57.605	1	24.18	O
ATOM	1527	CB	CYS A	189	−18.546	23.887	−58.776	1	24.76	C
ATOM	1528	SG	CYS A	189	−19.31	22.735	−59.952	1	29.58	S
ATOM	1529	H	CYS A	189	−19.448	26.286	−59.723	1	30.21	H
ATOM	1530	HA	CYS A	189	−20.214	24.548	−57.774	1	25.56	H
ATOM	1531	HB2	CYS A	189	−17.799	24.312	−59.224	1	29.72	H
ATOM	1532	HB3	CYS A	189	−18.222	23.367	−58.024	1	29.72	H
ATOM	1533	N	ALA A	190	−18.52	25.374	−56.053	1	21.28	N
ATOM	1534	CA	ALA A	190	−17.838	26.14	−55.015	1	21.57	C
ATOM	1535	C	ALA A	190	−16.767	25.316	−54.311	1	18.66	C
ATOM	1536	O	ALA A	190	−16.936	24.118	−54.073	1	17.27	O
ATOM	1537	CB	ALA A	190	−18.838	26.661	−54.007	1	20.73	C
ATOM	1538	H	ALA A	190	−18.759	24.585	−55.805	1	25.54	H
ATOM	1539	HA	ALA A	190	−17.403	26.904	−55.425	1	25.89	H
ATOM	1540	HB1	ALA A	190	−18.366	27.166	−53.327	1	24.88	H
ATOM	1541	HB2	ALA A	190	−19.476	27.232	−54.462	1	24.88	H
ATOM	1542	HB3	ALA A	190	−19.298	25.909	−53.602	1	24.88	H
ATOM	1543	N	LEU A	191	−15.664	25.981	−53.984	1	20.48	N
ATOM	1544	CA	LEU A	191	−14.578	25.382	−53.216	1	18.02	C
ATOM	1545	C	LEU A	191	−14.722	25.748	−51.745	1	17.63	C
ATOM	1546	O	LEU A	191	−14.852	26.927	−51.421	1	16.65	O
ATOM	1547	CB	LEU A	191	−13.226	25.869	−53.737	1	15.13	C
ATOM	1548	CG	LEU A	191	−12.856	25.493	−55.171	1	21.15	C
ATOM	1549	CD1	LEU A	191	−11.76	26.409	−55.687	1	23.95	C
ATOM	1550	CD2	LEU A	191	−12.414	24.04	−55.236	1	19.16	C
ATOM	1551	H	LEU A	191	−15.518	26.8	−54.2	1	24.57	H
ATOM	1552	HA	LEU A	191	−14.613	24.416	−53.3	1	21.63	H
ATOM	1553	HB2	LEU A	191	−13.213	26.837	−53.683	1	18.15	H
ATOM	1554	HB3	LEU A	191	−12.533	25.509	−53.16	1	18.15	H
ATOM	1555	HG	LEU A	191	−13.634	25.6	−55.741	1	25.38	H
ATOM	1556	HD11	LEU A	191	−11.54	26.155	−56.597	1	28.74	H
ATOM	1557	HD12	LEU A	191	−12.079	27.324	−55.667	1	28.74	H
ATOM	1558	HD13	LEU A	191	−10.979	26.317	−55.119	1	28.74	H
ATOM	1559	HD21	LEU A	191	−12.183	23.821	−56.153	1	22.99	H
ATOM	1560	HD22	LEU A	191	−11.641	23.919	−54.663	1	22.99	H
ATOM	1561	HD23	LEU A	191	−13.142	23.475	−54.934	1	22.99	H
ATOM	1562	N	TYR A	192	−14.703	24.757	−50.855	1	15.23	N
ATOM	1563	CA	TYR A	192	−14.718	25.056	−49.43	1	14.68	C
ATOM	1564	C	TYR A	192	−13.365	25.597	−48.98	1	17.4	C
ATOM	1565	O	TYR A	192	−12.324	25.129	−49.427	1	12.57	O
ATOM	1566	CB	TYR A	192	−15.055	23.831	−48.568	1	16.6	C
ATOM	1567	CG	TYR A	192	−14.916	24.199	−47.115	1	16.87	C
ATOM	1568	CD1	TYR A	192	−15.948	24.847	−46.45	1	14.23	C
ATOM	1569	CD2	TYR A	192	−13.724	23.981	−46.428	1	17.91	C
ATOM	1570	CE1	TYR A	192	−15.817	25.235	−45.14	1	15.45	C
ATOM	1571	CE2	TYR A	192	−13.584	24.368	−45.111	1	16.81	C
ATOM	1572	CZ	TYR A	192	−14.637	24.997	−44.473	1	17.95	C
ATOM	1573	OH	TYR A	192	−14.514	25.401	−43.164	1	18.94	O
ATOM	1574	H	TYR A	192	−14.683	23.919	−51.048	1	18.28	H
ATOM	1575	HA	TYR A	192	−15.386	25.737	−49.257	1	17.62	H
ATOM	1576	HB2	TYR A	192	−15.97	23.556	−48.734	1	19.92	H
ATOM	1577	HB3	TYR A	192	−14.437	23.11	−48.768	1	19.92	H
ATOM	1578	HD1	TYR A	192	−16.745	25.017	−46.898	1	17.07	H
ATOM	1579	HD2	TYR A	192	−13.015	23.564	−46.861	1	21.49	H
ATOM	1580	HE1	TYR A	192	−16.521	25.66	−44.706	1	18.54	H
ATOM	1581	HE2	TYR A	192	−12.788	24.21	−44.657	1	20.17	H
ATOM	1582	HH	TYR A	192	−13.753	25.2	−42.872	1	22.72	H
ATOM	1583	N	ALA A	193	−13.392	26.573	−48.078	1	14.04	N
ATOM	1584	CA	ALA A	193	−12.184	27.021	−47.395	1	14.46	C
ATOM	1585	C	ALA A	193	−12.528	27.614	−46.037	1	14.85	C
ATOM	1586	O	ALA A	193	−13.669	28.005	−45.784	1	16.32	O
ATOM	1587	CB	ALA A	193	−11.44	28.029	−48.233	1	16.01	C
ATOM	1588	H	ALA A	193	−14.103	26.995	−47.843	1	16.85	H
ATOM	1589	HA	ALA A	193	−11.6	26.26	−47.251	1	17.35	H
ATOM	1590	HB1	ALA A	193	−10.644	28.309	−47.756	1	19.22	H
ATOM	1591	HB2	ALA A	193	−11.194	27.617	−49.076	1	19.22	H
ATOM	1592	HB3	ALA A	193	−12.017	28.792	−48.393	1	19.22	H
ATOM	1593	N	SER A	194	−11.534	27.675	−45.162	1	13.15	N
ATOM	1594	CA	SER A	194	−11.726	28.278	−43.857	1	12.99	C
ATOM	1595	C	SER A	194	−11.964	29.777	−44.025	1	15.13	C
ATOM	1596	O	SER A	194	−11.387	30.378	−44.93	1	16.35	O
ATOM	1597	CB	SER A	194	−10.507	28.029	−42.963	1	15.47	C
ATOM	1598	OG	SER A	194	−10.547	28.856	−41.815	1	15.91	O
ATOM	1599	H	SER A	194	−10.741	27.374	−45.301	1	15.78	H
ATOM	1600	HA	SER A	194	−12.505	27.888	−43.431	1	15.59	H
ATOM	1601	HB2	SER A	194	−10.506	27.1	−42.684	1	18.57	H
ATOM	1602	HB3	SER A	194	−9.701	28.226	−43.466	1	18.57	H
ATOM	1603	HG	SER A	194	−9.875	28.71	−41.333	1	19.09	H
ATOM	1604	N	SER A	195	−12.803	30.394	−43.191	1	13.88	N
ATOM	1605	CA	SER A	195	−13.586	29.735	−42.148	1	14.38	C
ATOM	1606	C	SER A	195	−15.056	29.686	−42.571	1	18.17	C
ATOM	1607	O	SER A	195	−15.731	30.717	−42.606	1	15.7	O
ATOM	1608	CB	SER A	195	−13.442	30.477	−40.821	1	15.67	C
ATOM	1609	OG	SER A	195	−14.164	29.81	−39.798	1	20.71	O
ATOM	1610	H	SER A	195	−12.941	31.242	−43.215	1	16.65	H
ATOM	1611	HA	SER A	195	−13.268	28.826	−42.029	1	17.26	H
ATOM	1612	HB2	SER A	195	−12.503	30.51	−40.577	1	18.81	H
ATOM	1613	HB3	SER A	195	−13.791	31.376	−40.922	1	18.81	H
ATOM	1614	HG	SER A	195	−14.08	30.224	−39.071	1	24.86	H
ATOM	1615	N	PHE A	196	−15.542	28.492	−42.898	1	14.12	N
ATOM	1616	CA	PHE A	196	−16.912	28.314	−43.376	1	16.5	C
ATOM	1617	C	PHE A	196	−17.212	29.262	−44.53	1	16.82	C
ATOM	1618	O	PHE A	196	−18.205	29.992	−44.522	1	15.43	O
ATOM	1619	CB	PHE A	196	−17.909	28.514	−42.233	1	19.48	C
ATOM	1620	CG	PHE A	196	−17.9	27.392	−41.233	1	20.88	C
ATOM	1621	CD1	PHE A	196	−17.045	27.42	−40.146	1	19.36	C
ATOM	1622	CD2	PHE A	196	−18.734	26.3	−41.395	1	21	C
ATOM	1623	CE1	PHE A	196	−17.028	26.381	−39.233	1	22.54	C
ATOM	1624	CE2	PHE A	196	−18.722	25.259	−40.489	1	24.48	C
ATOM	1625	CZ	PHE A	196	−17.868	25.297	−39.409	1	23.71	C
ATOM	1626	H	PHE A	196	−15.093	27.76	−42.851	1	16.94	H
ATOM	1627	HA	PHE A	196	−17.014	27.407	−43.703	1	19.8	H
ATOM	1628	HB2	PHE A	196	−17.689	29.334	−41.763	1	23.38	H
ATOM	1629	HB3	PHE A	196	−18.803	28.576	−42.603	1	23.38	H
ATOM	1630	HD1	PHE A	196	−16.476	28.146	−40.027	1	23.23	H
ATOM	1631	HD2	PHE A	196	−19.31	26.267	−42.125	1	25.2	H
ATOM	1632	HE1	PHE A	196	−16.451	26.41	−38.504	1	27.05	H
ATOM	1633	HE2	PHE A	196	−19.29	24.532	−40.608	1	29.38	H
ATOM	1634	HZ	PHE A	196	−17.862	24.598	−38.795	1	28.45	H
ATOM	1635	N	LYS A		197	−16.328	29.24	−45.519	1	12.88	N
ATOM	1636	CA	LYS A	197	−16.488	30.028	−46.726	1	14.65	C
ATOM	1637	C	LYS A	197	−16.602	29.102	−47.924	1	20.06	C
ATOM	1638	O	LYS A	197	−16.201	27.937	−47.864	1	15.47	O
ATOM	1639	CB	LYS A	197	−15.316	30.995	−46.902	1	17.78	C
ATOM	1640	CG	LYS A	197	−15.28	32.1	−45.858	1	18.13	C
ATOM	1641	CD	LYS A	197	−14.046	32.976	−45.998	1	21.25	C
ATOM	1642	CE	LYS A	197	−14.128	34.17	−45.061	1	21.78	C
ATOM	1643	NZ	LYS A	197	−12.877	34.972	−45.042	1	22.18	N1+
ATOM	1644	H	LYS A	197	−15.612	28.764	−45.511	1	15.45	H
ATOM	1645	HA	LYS A	197	−17.305	30.547	−46.664	1	17.58	H
ATOM	1646	HB2	LYS A	197	−14.486	30.497	−46.837	1	21.34	H
ATOM	1647	HB3	LYS A	197	−15.382	31.413	−47.775	1	21.34	H
ATOM	1648	HG2	LYS A	197	−16.063	32.662	−45.962	1	21.75	H
ATOM	1649	HG3	LYS A	197	−15.269	31.702	−44.973	1	21.75	H
ATOM	1650	HD2	LYS A		197	−13.257	32.461	−45.77	1	25.49	H
ATOM	1651	HD3	LYS A		197	−13.985	33.305	−46.908	1	25.49	H
ATOM	1652	HE2	LYS A		197	−14.851	34.749	−45.349	1	26.13	H
ATOM	1653	HE3	LYS A		197	−14.295	33.854	−44.159	1	26.13	H
ATOM	1654	HZ1	LYS A		197	−12.703	35.282	−45.858	1	26.61	H
ATOM	1655	HZ2	LYS A	197	−12.965	35.659	−44.484	1	26.61	H
ATOM	1656	HZ3	LYS A	197	−12.196	34.466	−44.774	1	26.61	H
ATOM	1657	N	GLY A	198	−17.172	29.632	−49.001	1	21.19	N
ATOM	1658	CA	GLY A	198	−17.291	28.916	−50.256	1	20.02	C
ATOM	1659	C	GLY A	198	−16.977	29.862	−51.394	1	18.77	C
ATOM	1660	O	GLY A	198	−17.644	30.88	−51.561	1	21.65	O
ATOM	1661	H	GLY A	198	−17.505	30.424	−49.026	1	25.43	H
ATOM	1662	HA2	GLY A	198	−16.667	28.173	−50.278	1	24.02	H
ATOM	1663	HA3	GLY A	198	−18.193	28.577	−50.364	1	24.02	H
ATOM	1664	N	TYR A	199	−15.942	29.535	−52.16	1	17.44	N
ATOM	1665	CA	TYR A	199	−15.521	30.351	−53.289	1	16.54	C
ATOM	1666	C	TYR A	199	−16.048	29.768	−54.591	1	23.54	C
ATOM	1667	O	TYR A	199	−15.735	28.63	−54.944	1	19	O
ATOM	1668	CB	TYR A	199	−13.997	30.446	−53.349	1	17.44	C
ATOM	1669	CG	TYR A	199	−13.376	31.238	−52.222	1	14.05	C
ATOM	1670	CD1	TYR A	199	−13.236	30.689	−50.958	1	15.06	C
ATOM	1671	CD2	TYR A	199	−12.912	32.529	−52.432	1	17.4	C
ATOM	1672	CE1	TYR A	199	−12.663	31.41	−49.926	1	17.88	C
ATOM	1673	CE2	TYR A	199	−12.332	33.255	−51.409	1	15.39	C
ATOM	1674	CZ	TYR A	199	−12.213	32.69	−50.156	1	15.83	C
ATOM	1675	OH	TYR A	199	−11.637	33.406	−49.131	1	18.67	O
ATOM	1676	H	TYR A	199	−15.461	28.832	−52.043	1	20.93	H
ATOM	1677	HA	TYR A	199	−15.878	31.247	−53.189	1	19.84	H
ATOM	1678	HB2	TYR A	199	−13.629	29.549	−53.316	1	20.92	H
ATOM	1679	HB3	TYR A	199	−13.745	30.872	−54.183	1	20.92	H
ATOM	1680	HD1	TYR A	199	−13.541	29.825	−50.798	1	18.08	H
ATOM	1681	HD2	TYR A	199	−12.992	32.912	−53.275	1	20.88	H
ATOM	1682	HE1	TYR A	199	−12.579	31.03	−49.082	1	21.46	H
ATOM	1683	HE2	TYR A	199	−12.029	34.12	−51.564	1	18.47	H
ATOM	1684	HH	TYR A	199	−11.626	32.945	−48.429	1	22.4	H
ATOM	1685	N	ILE A	200	−16.841	30.552	−55.309	1	22.64	N
ATOM	1686	CA	ILE A	200	−17.424	30.09	−56.558	1	23.49	C
ATOM	1687	C	ILE A	200	−16.323	29.921	−57.6	1	24.43	C
ATOM	1688	O	ILE A	200	−15.491	30.808	−57.79	1	21.73	O
ATOM	1689	CB	ILE A	200	−18.499	31.059	−57.068	1	24.34	C
ATOM	1690	CG1	ILE A	200	−19.571	31.263	−55.989	1	24.68	C
ATOM	1691	CG2	ILE A	200	−19.121	30.526	−58.354	1	27.39	C
ATOM	1692	CD1	ILE A	200	−20.587	32.342	−56.308	1	32.82	C
ATOM	1693	H	ILE A	200	−17.058	31.356	−55.094	1	27.17	H
ATOM	1694	HA	ILE A	200	−17.84	29.226	−56.415	1	28.19	H
ATOM	1695	HB	ILE A	200	−18.082	31.915	−57.257	1	29.21	H
ATOM	1696	HG12	ILE A	200	−20.054	30.43	−55.87	1	29.61	H
ATOM	1697	HG13	ILE A	200	−19.133	31.508	−55.158	1	29.61	H
ATOM	1698	HG21	ILE A	200	−19.797	31.151	−58.66	1	32.86	H
ATOM	1699	HG22	ILE A	200	−18.427	30.433	−59.025	1	32.86	H
ATOM	1700	HG23	ILE A	200	−19.525	29.663	−58.174	1	32.86	H
ATOM	1701	HD11	ILE A	200	−21.223	32.403	−55.578	1	39.38	H
ATOM	1702	HD12	ILE A	200	−20.125	33.188	−56.417	1	39.38	H
ATOM	1703	HD13	ILE A	200	−21.048	32.108	−57.129	1	39.38	H
ATOM	1704	N	GLU A	201	−16.33	28.769	−58.264	1	22.73	N
ATOM	1705	CA	GLU A	201	−15.255	28.388	−59.169	1	24	C
ATOM	1706	C	GLU A	201	−15.8	27.657	−60.392	1	25.5	C
ATOM	1707	O	GLU A	201	−16.887	27.076	−60.35	1	22.4	O
ATOM	1708	CB	GLU A	201	−14.244	27.508	−58.425	1	23.12	C
ATOM	1709	CG	GLU A	201	−13.104	26.959	−59.269	1	25.67	C
ATOM	1710	CD	GLU A	201	−12.274	28.048	−59.917	1	31.64	C
ATOM	1711	OE1	GLU A	201	−11.116	28.247	−59.49	1	34.45	O
ATOM	1712	OE2	GLU A	201	−12.777	28.7	−60.856	1	31.63	O1−
ATOM	1713	H	GLU A	201	−16.957	28.184	−58.206	1	27.27	H
ATOM	1714	HA	GLU A	201	−14.797	29.186	−59.473	1	28.8	H
ATOM	1715	HB2	GLU A	201	−13.849	28.032	−57.71	1	27.75	H
ATOM	1716	HB3	GLU A	201	−14.716	26.75	−58.047	1	27.75	H
ATOM	1717	HG2	GLU A	201	−12.518	26.432	−58.704	1	30.81	H
ATOM	1718	HG3	GLU A	201	−13.472	26.404	−59.974	1	30.81	H
ATOM	1719	N	ASN A	202	−15.04	27.709	−61.48	1	26.48	N
ATOM	1720	CA	ASN A	202	−15.344	26.948	−62.684	1	25.56	C
ATOM	1721	C	ASN A	202	−15.316	25.452	−62.389	1	24.34	C
ATOM	1722	O	ASN A	202	−14.295	24.914	−61.967	1	26.28	O
ATOM	1723	CB	ASN A	202	−14.343	27.294	−63.788	1	29.63	C
ATOM	1724	CG	ASN A	202	−14.689	26.66	−65.123	1	31.7	C
ATOM	1725	OD1	ASN A	202	−15.292	25.589	−65.187	1	30.51	O
ATOM	1726	ND2	ASN A	202	−14.297	27.323	−66.203	1	38.46	N
ATOM	1727	H	ASN A	202	−14.328	28.187	−61.546	1	31.77	H
ATOM	1728	HA	ASN A	202	−16.234	27.18	−62.994	1	30.67	H
ATOM	1729	HB2	ASN A	202	−14.329	28.256	−63.91	1	35.55	H
ATOM	1730	HB3	ASN A	202	−13.464	26.98	−63.526	1	35.55	H
ATOM	1731	HD21	ASN A	202	−14.466	27.009	−66.985	1	46.15	H
ATOM	1732	HD22	ASN A	202	−13.873	28.067	−66.121	1	46.15	H
ATOM	1733	N	CYS A	203	−16.44	24.785	−62.627	1	28.75	N
ATOM	1734	CA	CYS A	203	−16.574	23.364	−62.325	1	25.56	C
ATOM	1735	C	CYS A	203	−15.508	22.513	−63.014	1	26.17	C
ATOM	1736	O	CYS A	203	−15.174	21.43	−62.539	1	23.9	O
ATOM	1737	CB	CYS A	203	−17.967	22.874	−62.726	1	25.82	C
ATOM	1738	SG	CYS A	203	−19.313	23.627	−61.778	1	33.04	S
ATOM	1739	H	CYS A	203	−17.148	25.136	−62.966	1	34.5	H
ATOM	1740	HA	CYS A	203	−16.479	23.238	−61.368	1	30.67	H
ATOM	1741	HB2	CYS A	203	−18.112	23.081	−63.663	1	30.99	H
ATOM	1742	HB3	CYS A	203	−18.011	21.914	−62.592	1	30.99	H
ATOM	1743	N	SER A	204	−14.962	23.015	−64.118	1	26.58	N
ATOM	1744	CA	SER A	204	−14.011	22.25	−64.918	1	28.83	C
ATOM	1745	C	SER A	204	−12.568	22.426	−64.464	1	29.48	C
ATOM	1746	O	SER A	204	−11.67	21.765	−64.98	1	30.84	O
ATOM	1747	CB	SER A	204	−14.13	22.646	−66.391	1	34.76	C
ATOM	1748	OG	SER A	204	−15.399	22.282	−66.905	1	36.78	O
ATOM	1749	H	SER A	204	−15.127	23.801	−64.426	1	31.89	H
ATOM	1750	HA	SER A	204	−14.23	21.308	−64.847	1	34.6	H
ATOM	1751	HB2	SER A	204	−14.02	23.607	−66.47	1	41.72	H
ATOM	1752	HB3	SER A	204	−13.44	22.19	−66.898	1	41.72	H
ATOM	1753	HG	SER A	204	−15.456	22.503	−67.713	1	44.13	H
ATOM	1754	N	THR A	205	−12.342	23.313	−63.501	1	30.18	N
ATOM	1755	CA	THR A	205	−10.991	23.564	−63.01	1	31.93	C
ATOM	1756	C	THR A	205	−10.595	22.49	−62.002	1	26.32	C
ATOM	1757	O	THR A	205	−11.3	22.28	−61.017	1	27.11	O
ATOM	1758	CB	THR A	205	−10.88	24.953	−62.354	1	30.33	C
ATOM	1759	OG1	THR A	205	−11.195	25.962	−63.322	1	32.74	O
ATOM	1760	CG2	THR A	205	−9.473	25.195	−61.822	1	28.31	C
ATOM	1761	H	THR A	205	−12.951	23.783	−63.117	1	36.22	H
ATOM	1762	HA	THR A	205	−10.369	23.528	−63.753	1	38.32	H
ATOM	1763	HB	THR A	205	−11.503	25.011	−61.613	1	36.4	H
ATOM	1764	HG1	THR A	205	−10.66	25.917	−63.968	1	39.29	H
ATOM	1765	HG21	THR A	205	−9.42	26.073	−61.413	1	33.97	H
ATOM	1766	HG22	THR A	205	−9.25	24.524	−61.158	1	33.97	H
ATOM	1767	HG23	THR A	205	−8.831	25.146	−62.547	1	33.97	H
ATOM	1768	N	PRO A	206	−9.462	21.808	−62.235	1	25.18	N
ATOM	1769	CA	PRO A	206	−9.108	20.744	−61.29	1	27.92	C
ATOM	1770	C	PRO A	206	−8.728	21.285	−59.913	1	27.31	C
ATOM	1771	O	PRO A	206	−8.02	22.285	−59.806	1	24.19	O
ATOM	1772	CB	PRO A	206	−7.918	20.051	−61.963	1	27.16	C
ATOM	1773	CG	PRO A	206	−7.34	21.073	−62.876	1	35.92	C
ATOM	1774	CD	PRO A	206	−8.479	21.937	−63.326	1	32.59	C
ATOM	1775	HA	PRO A	206	−9.839	20.113	−61.199	1	33.5	H
ATOM	1776	HB2	PRO A	206	−7.271	19.786	−61.29	1	32.59	H
ATOM	1777	HB3	PRO A	206	−8.229	19.28	−62.463	1	32.59	H
ATOM	1778	HG2	PRO A	206	−6.683	21.6	−62.396	1	43.11	H
ATOM	1779	HG3	PRO A	206	−6.93	20.631	−63.636	1	43.11	H
ATOM	1780	HD2	PRO A	206	−8.189	22.859	−63.411	1	39.11	H
ATOM	1781	HD3	PRO A	206	−8.85	21.602	−64.157	1	39.11	H
ATOM	1782	N	ASN A	207	−9.223	20.624	−58.873	1	24.26	N
ATOM	1783	CA	ASN A	207	−8.923	20.983	−57.492	1	25.76	C
ATOM	1784	C	ASN A	207	−8.955	19.741	−56.616	1	23.33	C
ATOM	1785	O	ASN A	207	−9.56	18.734	−56.988	1	20.6	O
ATOM	1786	CB	ASN A	207	−9.927	22.01	−56.957	1	23.82	C
ATOM	1787	CG	ASN A	207	−9.62	23.423	−57.405	1	27.43	C
ATOM	1788	OD1	ASN A	207	−8.771	24.097	−56.822	1	28.42	O
ATOM	1789	ND2	ASN A	207	−10.327	23.889	−58.43	1	23.94	N
ATOM	1790	H	ASN A	207	−9.749	19.947	−58.944	1	29.12	H
ATOM	1791	HA	ASN A	207	−8.034	21.369	−57.444	1	30.91	H
ATOM	1792	HB2	ASN A	207	−10.813	21.78	−57.276	1	28.58	H
ATOM	1793	HB3	ASN A	207	−9.909	21.993	−55.987	1	28.58	H
ATOM	1794	HD21	ASN A	207	−10.189	24.687	−58.721	1	28.73	H
ATOM	1795	HD22	ASN A	207	−10.923	23.393	−58.803	1	28.73	H
ATOM	1796	N	THR A	208	−8.312	19.815	−55.454	1	22.57	N
ATOM	1797	CA	THR A	208	−8.444	18.773	−54.443	1	19.78	C
ATOM	1798	C	THR A	208	−9.888	18.768	−53.954	1	16.39	C
ATOM	1799	O	THR A	208	−10.62	19.723	−54.195	1	15.26	O
ATOM	1800	CB	THR A	208	−7.479	18.998	−53.26	1	20.25	C
ATOM	1801	OG1	THR A	208	−7.743	20.271	−52.655	1	17.1	O
ATOM	1802	CG2	THR A	208	−6.032	18.957	−53.738	1	20.83	C
ATOM	1803	H	THR A	208	−7.792	20.461	−55.227	1	27.08	H
ATOM	1804	HA	THR A	208	−8.249	17.909	−54.84	1	23.73	H
ATOM	1805	HB	THR A	208	−7.605	18.296	−52.603	1	24.3	H
ATOM	1806	HG1	THR A	208	−7.219	20.397	−52.01	1	20.52	H
ATOM	1807	HG21	THR A	208	−5.432	19.099	−52.989	1	24.99	H
ATOM	1808	HG22	THR A	208	−5.839	18.094	−54.137	1	24.99	H
ATOM	1809	HG23	THR A	208	−5.881	19.65	−54.399	1	24.99	H
ATOM	1810	N	TYR A	209	−10.303	17.702	−53.277	1	16.05	N
ATOM	1811	CA	TYR A	209	−11.692	17.583	−52.843	1	17.55	C
ATOM	1812	C	TYR A	209	−11.836	16.812	−51.533	1	16.31	C
ATOM	1813	O	TYR A	209	−10.928	16.09	−51.112	1	16.24	O
ATOM	1814	CB	TYR A	209	−12.534	16.92	−53.941	1	17.25	C
ATOM	1815	CG	TYR A	209	−12.03	15.571	−54.393	1	14.62	C
ATOM	1816	CD1	TYR A	209	−10.964	15.467	−55.276	1	19.2	C
ATOM	1817	CD2	TYR A	209	−12.633	14.401	−53.955	1	18.23	C
ATOM	1818	CE1	TYR A	209	−10.499	14.234	−55.695	1	22.13	C
ATOM	1819	CE2	TYR A	209	−12.175	13.16	−54.372	1	21.56	C
ATOM	1820	CZ	TYR A	209	−11.107	13.085	−55.243	1	22.08	C
ATOM	1821	OH	TYR A	209	−10.644	11.857	−55.664	1	21.65	O
ATOM	1822	H	TYR A	209	−9.804	17.037	−53.057	1	19.26	H
ATOM	1823	HA	TYR A	209	−12.048	18.474	−52.698	1	21.06	H
ATOM	1824	HB2	TYR A	209	−13.437	16.8	−53.608	1	20.7	H
ATOM	1825	HB3	TYR A	209	−12.547	17.504	−54.716	1	20.7	H
ATOM	1826	HD1	TYR A	209	−10.548	16.24	−55.582	1	23.04	H
ATOM	1827	HD2	TYR A	209	−13.351	14.449	−53.366	1	21.87	H
ATOM	1828	HE1	TYR A	209	−9.78	14.182	−56.283	1	26.56	H
ATOM	1829	HE2	TYR A	209	−12.585	12.383	−54.067	1	25.87	H
ATOM	1830	HH	TYR A	209	−9.994	11.959	−56.187	1	25.99	H
ATOM	1831	N	ILE A	210	−12.986	16.991	−50.892	1	14.44	N
ATOM	1832	CA	ILE A	210	−13.276	16.355	−49.617	1	13.02	C
ATOM	1833	C	ILE A	210	−14.502	15.475	−49.75	1	14.98	C
ATOM	1834	O	ILE A	210	−15.563	15.937	−50.175	1	15.19	O
ATOM	1835	CB	ILE A	210	−13.52	17.394	−48.506	1	15.09	C
ATOM	1836	CG1	ILE A	210	−12.293	18.294	−48.337	1	18.45	C
ATOM	1837	CG2	ILE A	210	−13.86	16.695	−47.19	1	15.58	C
ATOM	1838	CD1	ILE A	210	−12.516	19.483	−47.404	1	16.93	C
ATOM	1839	H	ILE A	210	−13.625	17.487	−51.184	1	17.32	H
ATOM	1840	HA	ILE A	210	−12.526	15.798	−49.356	1	15.62	H
ATOM	1841	HB	ILE A	210	−14.274	17.948	−48.763	1	18.1	H
ATOM	1842	HG12	ILE A	210	−11.566	17.764	−47.974	1	22.14	H
ATOM	1843	HG13	ILE A	210	−12.042	18.643	−49.207	1	22.14	H
ATOM	1844	HG21	ILE A	210	−14.01	17.366	−46.506	1	18.7	H
ATOM	1845	HG22	ILE A	210	−14.662	16.164	−47.313	1	18.7	H
ATOM	1846	HG23	ILE A	210	−13.119	16.123	−46.936	1	18.7	H
ATOM	1847	HD11	ILE A	210	−11.697	20	−47.351	1	20.32	H
ATOM	1848	HD12	ILE A	210	−13.232	20.033	−47.758	1	20.32	H
ATOM	1849	HD13	ILE A	210	−12.756	19.153	−46.524	1	20.32	H
ATOM	1850	N	CYS A	211	−14.352	14.207	−49.383	1	13.79	N
ATOM	1851	CA	CYS A	211	−15.472	13.276	−49.363	1	18.54	C
ATOM	1852	C	CYS A	211	−15.996	13.147	−47.94	1	18.83	C
ATOM	1853	O	CYS A	211	−15.243	13.306	−46.976	1	15.68	O
ATOM	1854	CB	CYS A	211	−15.057	11.909	−49.912	1	19.87	C
ATOM	1855	SG	CYS A	211	−14.655	11.923	−51.673	1	23.9	S
ATOM	1856	H	CYS A	211	−13.604	13.859	−49.139	1	16.55	H
ATOM	1857	HA	CYS A	211	−16.186	13.623	−49.92	1	22.25	H
ATOM	1858	HB2	CYS A	211	−14.272	11.605	−49.431	1	23.84	H
ATOM	1859	HB3	CYS A	211	−15.787	11.284	−49.779	1	23.84	H
ATOM	1860	N	MET A	212	−17.29	12.865	−47.821	1	16.73	N
ATOM	1861	CA	MET A	212	−17.952	12.779	−46.527	1	19.25	C
ATOM	1862	C	MET A	212	−19.005	11.671	−46.513	1	21.41	C
ATOM	1863	O	MET A	212	−19.713	11.464	−47.5	1	24.33	O
ATOM	1864	CB	MET A	212	−18.598	14.124	−46.181	1	15.5	C
ATOM	1865	CG	MET A	212	−19.443	14.128	−44.912	1	19.16	C
ATOM	1866	SD	MET A	212	−20.263	15.719	−44.644	1	21.71	S
ATOM	1867	CE	MET A	212	−21.41	15.313	−43.333	1	26.47	C
ATOM	1868	H	MET A	212	−17.813	12.717	−48.487	1	20.08	H
ATOM	1869	HA	MET A	212	−17.286	12.586	−45.848	1	23.1	H
ATOM	1870	HB2	MET A	212	−17.896	14.783	−46.066	1	18.61	H
ATOM	1871	HB3	MET A	212	−19.174	14.388	−46.916	1	18.61	H
ATOM	1872	HG2	MET A	212	−20.127	13.444	−44.983	1	22.99	H
ATOM	1873	HG3	MET A	212	−18.871	13.951	−44.148	1	22.99	H
ATOM	1874	HE1	MET A	212	−21.917	16.107	−43.101	1	31.76	H
ATOM	1875	HE2	MET A	212	−22.009	14.616	−43.643	1	31.76	H
ATOM	1876	HE3	MET A	212	−20.91	15.002	−42.562	1	31.76	H
ATOM	1877	N	GLN A	213	−19.09	10.969	−45.385	1	18.51	N
ATOM	1878	CA	GLN A	213	−20.142	9.985	−45.123	1	26.68	C
ATOM	1879	C	GLN A	213	−20.849	10.345	−43.823	1	25.55	C
ATOM	1880	O	GLN A	213	−20.203	10.47	−42.781	1	22.83	O
ATOM	1881	CB	GLN A	213	−19.567	8.571	−45.017	1	26.14	C
ATOM	1882	CG	GLN A	213	−19.588	7.762	−46.297	1	36.07	C
ATOM	1883	CD	GLN A	213	−19.101	6.337	−46.08	1	35.95	C
ATOM	1884	OE1	GLN A	213	−19.049	5.856	−44.949	1	38.02	O
ATOM	1885	NE2	GLN A	213	−18.738	5.658	−47.164	1	33.49	N
ATOM	1886	H	GLN A	213	−18.531	11.047	−44.735	1	22.21	H
ATOM	1887	HA	GLN A	213	−20.79	10.003	−45.844	1	32.01	H
ATOM	1888	HB2	GLN A	213	−18.643	8.636	−44.729	1	31.37	H
ATOM	1889	HB3	GLN A	213	−20.079	8.081	−44.354	1	31.37	H
ATOM	1890	HG2	GLN A	213	−20.497	7.722	−46.634	1	43.28	H
ATOM	1891	HG3	GLN A	213	−19.008	8.184	−46.95	1	43.28	H
ATOM	1892	HE21	GLN A	213	−18.786	6.028	−47.939	1	40.19	H
ATOM	1893	HE22	GLN A	213	−18.456	4.849	−47.09	1	40.19	H
ATOM	1894	N	ARG A	214	−22.169	10.497	−43.875	1	30.78	N
ATOM	1895	CA	ARG A	214	−22.922	10.975	−42.717	1	39	C
ATOM	1896	C	ARG A	214	−23.6	9.833	−41.967	1	50.04	C
ATOM	1897	O	ARG A	214	−23.446	9.709	−40.749	1	47.2	O
ATOM	1898	CB	ARG A	214	−23.958	12.01	−43.156	1	48.11	C
ATOM	1899	CG	ARG A	214	−24.524	12.838	−42.013	1	41.27	C
ATOM	1900	CD	ARG A	214	−24.916	14.231	−42.48	1	41.95	C
ATOM	1901	NE	ARG A	214	−25.794	14.187	−43.648	1	45.75	N
ATOM	1902	CZ	ARG A	214	−26.622	15.164	−44.006	1	46.72	C
ATOM	1903	NH1	ARG A	214	−26.706	16.278	−43.285	1	46.09	N
ATOM	1904	NH2	ARG A	214	−27.378	15.022	−45.084	1	46.67	N
ATOM	1905	H	ARG A	214	−22.653	10.331	−44.566	1	36.93	H
ATOM	1906	HA	ARG A	214	−22.31	11.41	−42.104	1	46.8	H
ATOM	1907	HB2	ARG A	214	−23.543	12.619	−43.786	1	57.73	H
ATOM	1908	HB3	ARG A	214	−24.698	11.55	−43.582	1	57.73	H
ATOM	1909	HG2	ARG A	214	−25.315	12.401	−41.661	1	49.52	H
ATOM	1910	HG3	ARG A	214	−23.852	12.928	−41.319	1	49.52	H
ATOM	1911	HD2	ARG A	214	−25.387	14.686	−41.765	1	50.35	H
ATOM	1912	HD3	ARG A	214	−24.116	14.723	−42.721	1	50.35	H
ATOM	1913	HE	ARG A	214	−25.774	13.48	−44.137	1	54.9	H
ATOM	1914	HH11	ARG A	214	−26.219	16.374	−42.584	1	55.31	H
ATOM	1915	HH12	ARG A	214	−27.246	16.904	−43.523	1	55.31	H
ATOM	1916	HH21	ARG A	214	−27.328	14.302	−45.553	1	56.01	H
ATOM	1917	HH22	ARG A	214	−27.916	15.651	−45.318	1	56.01	H
ATOM	1918	N	THR A	215	−24.349	9.007	−42.691	1	58.9	N
ATOM	1919	CA	THR A	215	−24.978	7.827	−42.103	1	68.61	C
ATOM	1920	C	THR A	215	−25.559	6.955	−43.21	1	64.97	C
ATOM	1921	O	THR A	215	−26.049	7.466	−44.216	1	62.09	O
ATOM	1922	CB	THR A	215	−26.083	8.217	−41.083	1	70.62	C
ATOM	1923	OG1	THR A	215	−25.689	7.809	−39.767	1	63.52	O
ATOM	1924	CG2	THR A	215	−27.433	7.574	−41.417	1	62.01	C
ATOM	1925	H	THR A	215	−24.51	9.108	−43.53	1	70.68	H
ATOM	1926	HA	THR A	215	−24.304	7.31	−41.635	1	82.33	H
ATOM	1927	HB	THR A	215	−26.198	9.18	−41.094	1	84.75	H
ATOM	1928	HG1	THR A	215	−26.283	8.018	−39.211	1	76.23	H
ATOM	1929	HG21	THR A	215	−27.35	6.608	−41.411	1	74.41	H
ATOM	1930	HG22	THR A	215	−28.097	7.839	−40.761	1	74.41	H
ATOM	1931	HG23	THR A	215	−27.727	7.86	−42.296	1	74.41	H
TER	1932		THR A	215
ATOM	1933	N	SER B	94	−17.256	−1.068	−39.057	1	38.91	N
ATOM	1934	CA	SER B	94	−16.499	−1.068	−37.812	1	42.58	C
ATOM	1935	C	SER B	94	−16.281	0.359	−37.313	1	42.15	C
ATOM	1936	O	SER B	94	−16.626	1.322	−37.999	1	37.44	O
ATOM	1937	CB	SER B	94	−15.156	−1.775	−37.999	1	45.61	C
ATOM	1938	OG	SER B	94	−14.385	−1.141	−39.004	1	54.06	O
ATOM	1939	HA	SER B	94	−17.001	−1.549	−37.136	1	51.1	H
ATOM	1940	HB2	SER B	94	−14.667	−1.748	−37.162	1	54.73	H
ATOM	1941	HB3	SER B	94	−15.318	−2.695	−38.259	1	54.73	H
ATOM	1942	HG	SER B	94	−14.237	−0.342	−38.791	1	64.88	H
ATOM	1943	N	TYR B	95	−15.698	0.478	−36.122	1	37.34	N
ATOM	1944	CA	TYR B	95	−15.564	1.76	−35.437	1	35.53	C
ATOM	1945	C	TYR B	95	−14.114	2.137	−35.164	1	36.3	C
ATOM	1946	O	TYR B	95	−13.233	1.279	−35.095	1	36.5	O
ATOM	1947	CB	TYR B	95	−16.332	1.732	−34.113	1	34.25	C
ATOM	1948	CG	TYR B	95	−17.832	1.686	−34.273	1	32.06	C
ATOM	1949	CD1	TYR B	95	−18.476	0.505	−34.615	1	35.96	C
ATOM	1950	CD2	TYR B	95	−18.604	2.822	−34.078	1	33.01	C
ATOM	1951	CE1	TYR B	95	−19.848	0.458	−34.761	1	34.2	C
ATOM	1952	CE2	TYR B	95	−19.976	2.784	−34.22	1	40.01	C
ATOM	1953	CZ	TYR B	95	−20.593	1.601	−34.563	1	39.11	C
ATOM	1954	OH	TYR B	95	−21.96	1.564	−34.706	1	42	O
ATOM	1955	H	TYR B	95	−15.367	−0.183	−35.682	1	44.8	H
ATOM	1956	HA	TYR B	95	−15.953	2.454	−35.992	1	42.63	H
ATOM	1957	HB2	TYR B	95	−16.063	0.945	−33.614	1	41.11	H
ATOM	1958	HB3	TYR B	95	−16.113	2.531	−33.608	1	41.11	H
ATOM	1959	HD1	TYR B	95	−17.975	−0.267	−34.749	1	43.16	H
ATOM	1960	HD2	TYR B	95	−18.191	3.622	−33.847	1	39.62	H
ATOM	1961	HE1	TYR B	95	−20.267	−0.339	−34.991	1	41.04	H
ATOM	1962	HE2	TYR B	95	−20.482	3.554	−34.088	1	48.01	H
ATOM	1963	HH	TYR B	95	−22.285	2.324	−34.558	1	50.4	H
ATOM	1964	N	CYS B	96	−13.888	3.438	−35.01	1	30.02	N
ATOM	1965	CA	CYS B	96	−12.593	3.973	−34.613	1	34.28	C
ATOM	1966	C	CYS B	96	−12.642	4.321	−33.129	1	32.78	C
ATOM	1967	O	CYS B	96	−13.603	4.937	−32.669	1	31.3	O
ATOM	1968	CB	CYS B	96	−12.247	5.206	−35.453	1	31.86	C
ATOM	1969	SG	CYS B	96	−10.576	5.848	−35.221	1	33.72	S
ATOM	1970	H	CYS B	96	−14.485	4.044	−35.133	1	36.02	H
ATOM	1971	HA	CYS B	96	−11.907	3.302	−34.752	1	41.13	H
ATOM	1972	HB2	CYS B	96	−12.345	4.977	−36.391	1	38.23	H
ATOM	1973	HB3	CYS B	96	−12.867	5.917	−35.227	1	38.23	H
ATOM	1974	N	GLY B	97	−11.618	3.918	−32.381	1	33.09	N
ATOM	1975	CA	GLY B	97	−11.554	4.204	−30.957	1	31.22	C
ATOM	1976	C	GLY B	97	−11.135	2.998	−30.132	1	35.55	C
ATOM	1977	O	GLY B	97	−10.551	2.054	−30.663	1	39.96	O
ATOM	1978	H	GLY B	97	−10.944	3.474	−32.68	1	39.71	H
ATOM	1979	HA2	GLY B	97	−10.917	4.918	−30.8	1	37.46	H
ATOM	1980	HA3	GLY B	97	−12.426	4.497	−30.648	1	37.46	H
ATOM	1981	N	PRO B	98	−11.429	3.019	−28.821	1	38.2	N
ATOM	1982	CA	PRO B	98	−12.139	4.096	−28.12	1	36.03	C
ATOM	1983	C	PRO B	98	−11.312	5.373	−27.973	1	35.11	C
ATOM	1984	O	PRO B	98	−10.086	5.318	−27.863	1	34.34	O
ATOM	1985	CB	PRO B	98	−12.439	3.48	−26.749	1	43.03	C
ATOM	1986	CG	PRO B	98	−11.379	2.466	−26.551	1	44.9	C
ATOM	1987	CD	PRO B	98	−11.075	1.914	−27.912	1	43.35	C
ATOM	1988	HA	PRO B	98	−12.973	4.301	−28.57	1	43.23	H
ATOM	1989	HB2	PRO B	98	−12.392	4.165	−26.065	1	51.64	H
ATOM	1990	HB3	PRO B	98	−13.315	3.064	−26.761	1	51.64	H
ATOM	1991	HG2	PRO B	98	−10.593	2.888	−26.172	1	53.88	H
ATOM	1992	HG3	PRO B	98	−11.706	1.765	−25.965	1	53.88	H
ATOM	1993	HD2	PRO B	98	−10.131	1.703	−27.988	1	52.02	H
ATOM	1994	HD3	PRO B	98	−11.628	1.138	−28.093	1	52.02	H
ATOM	1995	N	CYS B	99	−11.999	6.51	−27.991	1	28.31	N
ATOM	1996	CA	CYS B	99	−11.382	7.814	−27.782	1	31.04	C
ATOM	1997	C	CYS B	99	−12.176	8.587	−26.75	1	29.57	C
ATOM	1998	O	CYS B	99	−13.297	8.207	−26.419	1	34.43	O
ATOM	1999	CB	CYS B	99	−11.33	8.62	−29.08	1	22.49	C
ATOM	2000	SG	CYS B	99	−10.222	7.973	−30.33	1	25.81	S
ATOM	2001	H	CYS B	99	−12.847	6.552	−28.127	1	33.97	H
ATOM	2002	HA	CYS B	99	−10.477	7.697	−27.453	1	37.25	H
ATOM	2003	HB2	CYS B	99	−12.22	8.645	−29.464	1	26.99	H
ATOM	2004	HB3	CYS B	99	−11.04	9.522	−28.872	1	26.99	H
ATOM	2005	N	PRO B	100	−11.599	9.682	−26.237	1	32.75	N
ATOM	2006	CA	PRO B	100	−12.421	10.607	−25.458	1	27.02	C
ATOM	2007	C	PRO B	100	−13.576	11.111	−26.308	1	29.55	C
ATOM	2008	O	PRO B	100	−13.455	11.152	−27.535	1	23.9	O
ATOM	2009	CB	PRO B	100	−11.45	11.733	−25.099	1	26.53	C
ATOM	2010	CG	PRO B	100	−10.094	11.101	−25.168	1	24.03	C
ATOM	2011	CD	PRO B	100	−10.181	10.084	−26.262	1	29.2	C
ATOM	2012	HA	PRO B	100	−12.756	10.184	−24.652	1	32.42	H
ATOM	2013	HB2	PRO B	100	−11.528	12.452	−25.745	1	31.83	H
ATOM	2014	HB3	PRO B	100	−11.635	12.053	−24.202	1	31.83	H
ATOM	2015	HG2	PRO B	100	−9.431	11.776	−25.381	1	28.84	H
ATOM	2016	HG3	PRO B	100	−9.89	10.676	−24.321	1	28.84	H
ATOM	2017	HD2	PRO B	100	−9.957	10.486	−27.116	1	35.04	H
ATOM	2018	HD3	PRO B	100	−9.61	9.325	−26.064	1	35.04	H
ATOM	2019	N	LYS B	101	−14.678	11.479	−25.668	1	32.78	N
ATOM	2020	CA	LYS B	101	−15.875	11.896	−26.387	1	39.36	C
ATOM	2021	C	LYS B	101	−15.597	13.072	−27.325	1	32.37	C
ATOM	2022	O	LYS B	101	−14.877	14.005	−26.97	1	30.08	O
ATOM	2023	CB	LYS B	101	−16.984	12.266	−25.396	1	44.44	C
ATOM	2024	CG	LYS B	101	−18.332	12.57	−26.041	1	61.82	C
ATOM	2025	CD	LYS B	101	−18.865	11.378	−26.824	1	74.76	C
ATOM	2026	CE	LYS B	101	−20.227	11.667	−27.429	1	100.45	C
ATOM	2027	NZ	LYS B	101	−20.686	10.552	−28.301	1	117.51	N1+
ATOM	2028	H	LYS B		101	−14.76	11.497	−24.812	1	39.34	H
ATOM	2029	HA	LYS B	101	−16.192	11.153	−26.926	1	47.24	H
ATOM	2030	HB2	LYS B	101	−17.111	11.525	−24.782	1	53.33	H
ATOM	2031	HB3	LYS B	101	−16.709	13.054	−24.903	1	53.33	H
ATOM	2032	HG2	LYS B		101	−18.975	12.79	−25.348	1	74.18	H
ATOM	2033	HG3	LYS B		101	−18.232	13.315	−26.654	1	74.18	H
ATOM	2034	HD2	LYS B		101	−18.251	11.169	−27.546	1	89.71	H
ATOM	2035	HD3	LYS B	101	−18.953	10.617	−26.228	1	89.71	H
ATOM	2036	HE2	LYS B		101	−20.876	11.782	−26.716	1	120.53	H
ATOM	2037	HE3	LYS B		101	−20.174	12.472	−27.967	1	120.53	H
ATOM	2038	HZ1	LYS B	101	−21.485	10.743	−28.644	1	141.01	H
ATOM	2039	HZ2	LYS B	101	−20.108	10.429	−28.967	1	141.01	H
ATOM	2040	HZ3	LYS B		101	−20.747	9.8	−27.828	1	141.01	H
ATOM	2041	N	ASN B	102	−16.163	12.996	−28.527	1	30.16	N
ATOM	2042	CA	ASN B	102	−16.115	14.077	−29.514	1	31.24	C
ATOM	2043	C	ASN B	102	−14.712	14.442	−30.002	1	27.87	C
ATOM	2044	O	ASN B	102	−14.519	15.491	−30.613	1	26.23	O
ATOM	2045	CB	ASN B	102	−16.798	15.329	−28.954	1	34.75	C
ATOM	2046	CG	ASN B	102	−18.292	15.143	−28.774	1	42.54	C
ATOM	2047	OD1	ASN B	102	−18.922	14.366	−29.491	1	45.19	O
ATOM	2048	ND2	ASN B	102	−18.866	15.857	−27.814	1	46.35	N
ATOM	2049	H	ASN B	102	−16.596	12.306	−28.804	1	36.19	H
ATOM	2050	HA	ASN B	102	−16.623	13.797	−30.292	1	37.49	H
ATOM	2051	HB2	ASN B	102	−16.414	15.538	−28.088	1	41.7	H
ATOM	2052	HB3	ASN B	102	−16.659	16.067	−29.567	1	41.7	H
ATOM	2053	HD21	ASN B	102	−19.712	15.786	−27.673	1	55.63	H
ATOM	2054	HD22	ASN B	102	−18.394	16.391	−27.333	1	55.63	H
ATOM	2055	N	TRP B	103	−13.737	13.577	−29.751	1	23.28	N
ATOM	2056	CA	TRP B	103	−12.41	13.762	−30.328	1	23.16	C
ATOM	2057	C	TRP B	103	−12.392	13.237	−31.763	1	23.53	C
ATOM	2058	O	TRP B	103	−13.233	12.419	−32.14	1	22.63	O
ATOM	2059	CB	TRP B	103	−11.343	13.049	−29.491	1	21.69	C
ATOM	2060	CG	TRP B	103	−10.963	13.783	−28.236	1	23.99	C
ATOM	2061	CD1	TRP B	103	−11.76	14.599	−27.485	1	23.75	C
ATOM	2062	CD2	TRP B	103	−9.679	13.777	−27.595	1	20.75	C
ATOM	2063	NE1	TRP B	103	−11.054	15.094	−26.413	1	20.78	N
ATOM	2064	CE2	TRP B	103	−9.775	14.606	−26.459	1	20.29	C
ATOM	2065	CE3	TRP B	103	−8.461	13.15	−27.871	1	21.26	C
ATOM	2066	CZ2	TRP B	103	−8.699	14.823	−25.6	1	21.46	C
ATOM	2067	CZ3	TRP B	103	−7.394	13.365	−27.015	1	25.01	C
ATOM	2068	CH2	TRP B	103	−7.521	14.195	−25.893	1	17.81	C
ATOM	2069	H	TRP B	103	−13.815	12.881	−29.253	1	27.94	H
ATOM	2070	HA	TRP B	103	−12.198	14.708	−30.348	1	27.79	H
ATOM	2071	HB2	TRP B	103	−11.68	12.176	−29.233	1	26.03	H
ATOM	2072	HB3	TRP B	103	−10.542	12.946	−30.028	1	26.03	H
ATOM	2073	HD1	TRP B	103	−12.652	14.789	−27.67	1	28.5	H
ATOM	2074	HE1	TRP B	103	−11.365	15.626	−25.813	1	24.94	H
ATOM	2075	HE3	TRP B	103	−8.37	12.597	−28.613	1	25.51	H
ATOM	2076	HZ2	TRP B	103	−8.781	15.373	−24.854	1	25.75	H
ATOM	2077	HZ3	TRP B	103	−6.578	12.953	−27.188	1	30.01	H
ATOM	2078	HH2	TRP B	103	−6.787	14.323	−25.336	1	21.37	H
ATOM	2079	N	ILE B	104	−11.452	13.725	−32.566	1	17.2	N
ATOM	2080	CA	ILE B	104	−11.198	13.133	−33.873	1	21.24	C
ATOM	2081	C	ILE B	104	−10.616	11.753	−33.647	1	24.16	C
ATOM	2082	O	ILE B	104	−9.835	11.559	−32.719	1	23.98	O
ATOM	2083	CB	ILE B	104	−10.215	13.966	−34.726	1	21.34	C
ATOM	2084	CG1	ILE B	104	−10.796	15.348	−35.026	1	22.32	C
ATOM	2085	CG2	ILE B	104	−9.876	13.23	−36.033	1	24.29	C
ATOM	2086	CD1	ILE B	104	−9.849	16.253	−35.781	1	28.99	C
ATOM	2087	H	ILE B	104	−10.949	14.396	−32.377	1	20.64	H
ATOM	2088	HA	ILE B	104	−12.032	13.044	−34.359	1	25.48	H
ATOM	2089	HB	ILE B	104	−9.395	14.083	−34.221	1	25.61	H
ATOM	2090	HG12	ILE B	104	−11.597	15.241	−35.564	1	26.78	H
ATOM	2091	HG13	ILE B	104	−11.018	15.783	−34.188	1	26.78	H
ATOM	2092	HG21	ILE B	104	−9.259	13.772	−36.55	1	29.15	H
ATOM	2093	HG22	ILE B	104	−9.467	12.377	−35.818	1	29.15	H
ATOM	2094	HG23	ILE B	104	−10.693	13.088	−36.536	1	29.15	H
ATOM	2095	HD11	ILE B	104	−10.283	17.107	−35.934	1	34.79	H
ATOM	2096	HD12	ILE B	104	−9.046	16.381	−35.252	1	34.79	H
ATOM	2097	HD13	ILE B	104	−9.624	15.839	−36.628	1	34.79	H
ATOM	2098	N	CYS B	105	−11.001	10.8	−34.489	1	22.22	N
ATOM	2099	CA	CYS B	105	−10.421	9.462	−34.455	1	24.13	C
ATOM	2100	C	CYS B	105	−9.93	9.12	−35.853	1	25.68	C
ATOM	2101	O	CYS B	105	−10.66	9.288	−36.83	1	25.12	O
ATOM	2102	CB	CYS B	105	−11.44	8.433	−33.962	1	25.61	C
ATOM	2103	SG	CYS B	105	−10.702	6.857	−33.461	1	33.63	S
ATOM	2104	H	CYS B	105	−11.602	10.904	−35.096	1	26.67	H
ATOM	2105	HA	CYS B	105	−9.661	9.455	−33.852	1	28.95	H
ATOM	2106	HB2	CYS B	105	−11.908	8.799	−33.195	1	30.73	H
ATOM	2107	HB3	CYS B	105	−12.071	8.251	−34.676	1	30.73	H
ATOM	2108	N	TYR B	106	−8.689	8.653	−35.949	1	22.66	N
ATOM	2109	CA	TYR B	106	−8.061	8.421	−37.245	1	21.9	C
ATOM	2110	C	TYR B	106	6.84	7.512	−37.14	1	29.8	C
ATOM	2111	O	TYR B	106	−5.832	7.876	−36.531	1	19.08	O
ATOM	2112	CB	TYR B	106	−7.656	9.754	−37.874	1	22.79	C
ATOM	2113	CG	TYR B	106	−7.09	9.639	−39.271	1	21.75	C
ATOM	2114	CD1	TYR B	106	−7.886	9.228	−40.333	1	23	C
ATOM	2115	CD2	TYR B	106	−5.766	9.961	−39.532	1	22.3	C
ATOM	2116	CE1	TYR B	106	−7.375	9.131	−41.614	1	22.33	C
ATOM	2117	CE2	TYR B	106	−5.247	9.871	−40.811	1	23.29	C
ATOM	2118	CZ	TYR B	106	−6.056	9.455	−41.846	1	24.28	C
ATOM	2119	OH	TYR B	106	−5.543	9.363	−43.116	1	28.23	O
ATOM	2120	H	TYR B	106	−8.188	8.462	−35.277	1	27.19	H
ATOM	2121	HA	TYR B	106	−8.703	7.995	−37.834	1	26.28	H
ATOM	2122	HB2	TYR B	106	−8.438	10.326	−37.919	1	27.35	H
ATOM	2123	HB3	TYR B	106	−6.98	10.168	−37.315	1	27.35	H
ATOM	2124	HD1	TYR B	106	−8.777	9.01	−40.179	1	27.6	H
ATOM	2125	HD2	TYR B	106	−5.218	10.244	−38.836	1	26.77	H
ATOM	2126	HE1	TYR B	106	−7.919	8.852	−42.315	1	26.8	H
ATOM	2127	HE2	TYR B	106	−4.357	10.087	−40.97	1	27.94	H
ATOM	2128	HH	TYR B	106	4.733	9.588	−43.115	1	33.88	H
ATOM	2129	N	LYS B	107	6.944	6.335	−37.75	1	26.75	N
ATOM	2130	CA	LYS B	107	−5.852	5.367	−37.787	1	26.22	C
ATOM	2131	C	LYS B	107	−5.272	5.107	−36.397	1	26.74	C
ATOM	2132	O	LYS B	107	−4.095	5.36	−36.145	1	26.52	O
ATOM	2133	CB	LYS B	107	−4.763	5.846	−38.749	1	24.14	C
ATOM	2134	CG	LYS B	107	−5.256	5.963	−40.189	1	25.22	C
ATOM	2135	CD	LYS B	107	−4.169	6.41	−41.147	1	30.82	C
ATOM	2136	CE	LYS B	107	−4.65	6.327	−42.592	1	28.59	C
ATOM	2137	NZ	LYS B	107	−3.633	6.838	−43.557	1	32.24	N1+
ATOM	2138	H	LYS B	107	−7.653	6.068	−38.157	1	32.1	H
ATOM	2139	HA	LYS B	107	−6.195	4.525	−38.126	1	31.46	H
ATOM	2140	HB2	LYS B	107	−4.453	6.721	−38.466	1	28.97	H
ATOM	2141	HB3	LYS B	107	−4.027	5.214	−38.734	1	28.97	H
ATOM	2142	HG2	LYS B		107	−5.578	5.097	−40.483	1	30.27	H
ATOM	2143	HG3	LYS B		107	−5.974	6.614	−40.224	1	30.27	H
ATOM	2144	HD2	LYS B	107	−3.93	7.331	−40.957	1	36.98	H
ATOM	2145	HD3	LYS B	107	−3.395	5.834	−41.049	1	36.98	H
ATOM	2146	HE2	LYS B	107	−4.836	5.401	−42.812	1	34.3	H
ATOM	2147	HE3	LYS B		107	−5.453	6.861	−42.69	1	34.3	H
ATOM	2148	HZ1	LYS B	107	−3.448	7.69	−43.381	1	38.69	H
ATOM	2149	HZ2	LYS B	107	−2.885	6.36	−43.491	1	38.69	H
ATOM	2150	HZ3	LYS B	107	−3.944	6.775	−44.388	1	38.69	H
ATOM	2151	N	ASN B	108	−6.125	4.609	−35.505	1	28.96	N
ATOM	2152	CA	ASN B	108	−5.729	4.193	−34.16	1	35.2	C
ATOM	2153	C	ASN B	108	5.175	5.334	−33.306	1	33.16	C
ATOM	2154	O	ASN B	108	−4.472	5.094	−32.324	1	35.7	O
ATOM	2155	CB	ASN B	108	−4.701	3.058	−34.243	1	34	C
ATOM	2156	CG	ASN B	108	−5.251	1.82	−34.927	1	38.47	C
ATOM	2157	OD1	ASN B	108	−6.448	1.54	−34.861	1	40.72	O
ATOM	2158	ND2	ASN B	108	4.377	1.071	−35.589	1	50.98	N
ATOM	2159	H	ASN B	108	−6.964	4.5	−35.66	1	34.75	H
ATOM	2160	HA	ASN B	108	−6.512	3.844	−33.705	1	42.24	H
ATOM	2161	HB2	ASN B	108	−3.932	3.364	−34.749	1	40.8	H
ATOM	2162	HB3	ASN B	108	−4.43	2.81	−33.345	1	40.8	H
ATOM	2163	HD21	ASN B	108	−4.64	0.359	−35.993	1	61.17	H
ATOM	2164	HD22	ASN B	108	−3.548	1.298	−35.613	1	61.17	H
ATOM	2165	N	ASN B	109	−5.499	6.57	−33.679	1	26.48	N
ATOM	2166	CA	ASN B	109	−5.125	7.739	−32.888	1	25.08	C
ATOM	2167	C	ASN B	109	−6.311	8.665	−32.655	1	23.92	C
ATOM	2168	O	ASN B	109	−7.165	8.828	−33.526	1	25.78	O
ATOM	2169	CB	ASN B	109	−3.994	8.508	−33.571	1	25.68	C
ATOM	2170	CG	ASN B	109	−2.706	7.718	−33.624	1	28.52	C
ATOM	2171	OD1	ASN B	109	−2.107	7.55	−34.686	1	29.25	O
ATOM	2172	ND2	ASN B	109	−2.278	7.221	−32.474	1	28.6	N
ATOM	2173	H	ASN B	109	−5.94	6.759	−34.393	1	31.78	H
ATOM	2174	HA	ASN B	109	−4.804	7.442	−32.022	1	30.1	H
ATOM	2175	HB2	ASN B	109	−4.257	8.715	−34.482	1	30.82	H
ATOM	2176	HB3	ASN B	109	−3.825	9.326	−33.079	1	30.82	H
ATOM	2177	HD21	ASN B	109	−1.551	6.763	−32.448	1	34.32	H
ATOM	2178	HD22	ASN B	109	2.728	7.355	−31.753	1	34.32	H
ATOM	2179	N	CYS B	110	−6.355	9.262	−31.467	1	21.75	N
ATOM	2180	CA	CYS B	110	−7.381	10.236	−31.115	1	19.96	C
ATOM	2181	C	CYS B	110	−6.754	11.621	−31.065	1	20.85	C
ATOM	2182	O	CYS B	110	−5.632	11.768	−30.591	1	18.06	O
ATOM	2183	CB	CYS B	110	−8.015	9.899	−29.766	1	23.36	C
ATOM	2184	SG	CYS B	110	−8.365	8.144	−29.523	1	28.07	S
ATOM	2185	H	CYS B	110	−5.789	9.116	−30.836	1	26.1	H
ATOM	2186	HA	CYS B	110	−8.076	10.235	−31.792	1	23.95	H
ATOM	2187	HB2	CYS B	110	−7.411	10.18	−29.061	1	28.03	H
ATOM	2188	HB3	CYS B	110	−8.854	10.38	−29.689	1	28.03	H
ATOM	2189	N	TYR B	111	−7.475	12.626	−31.554	1	18.22	N
ATOM	2190	CA	TYR B	111	−6.973	13.997	−31.572	1	16.26	C
ATOM	2191	C	TYR B	111	−8.02	14.998	−31.11	1	18.87	C
ATOM	2192	O	TYR B	111	−9.212	14.83	−31.37	1	17.84	O
ATOM	2193	CB	TYR B	111	−6.517	14.392	−32.977	1	16.69	C
ATOM	2194	CG	TYR B	111	−5.434	13.532	−33.571	1	17.24	C
ATOM	2195	CD1	TYR B	111	−4.095	13.773	−33.292	1	20.23	C
ATOM	2196	CD2	TYR B	111	−5.747	12.493	−34.436	1	19.87	C
ATOM	2197	CE1	TYR B	111	−3.102	12.992	−33.843	1	17.86	C
ATOM	2198	CE2	TYR B	111	−4.763	11.71	−34.994	1	19.29	C
ATOM	2199	CZ	TYR B	111	−3.443	11.962	−34.696	1	19.83	C
ATOM	2200	OH	TYR B	111	−2.463	11.177	−35.251	1	21.43	O
ATOM	2201	H	TYR B	111	−8.264	12.539	−31.884	1	21.87	H
ATOM	2202	HA	TYR B	111	−6.209	14.064	−30.977	1	19.51	H
ATOM	2203	HB2	TYR B	111	−7.282	14.349	−33.571	1	20.03	H
ATOM	2204	HB3	TYR B	111	−6.181	15.302	−32.947	1	20.03	H
ATOM	2205	HD1	TYR B	111	−3.865	14.467	−32.717	1	24.28	H
ATOM	2206	HD2	TYR B	111	−6.638	12.321	−34.639	1	23.85	H
ATOM	2207	HE1	TYR B	111	−2.21	13.16	−33.644	1	21.44	H
ATOM	2208	HE2	TYR B	111	−4.988	11.013	−35.568	1	23.14	H
ATOM	2209	HH	TYR B	111	−2.809	10.593	−35.746	1	25.72	H
ATOM	2210	N	GLN B	112	−7.573	16.055	−30.444	1	16.37	N
ATOM	2211	CA	GLN B	112	−8.44	17.199	−30.183	1	18.53	C
ATOM	2212	C	GLN B	112	−7.66	18.496	−30.315	1	18.9	C
ATOM	2213	O	GLN B	112	−6.506	18.591	−29.89	1	13.32	O
ATOM	2214	CB	GLN B	112	−9.083	17.104	−28.798	1	18.31	C
ATOM	2215	CG	GLN B	112	−10.016	18.266	−28.458	1	20.42	C
ATOM	2216	CD	GLN B	112	−11.205	18.373	−29.402	1	22.22	C
ATOM	2217	OE1	GLN B	112	−11.057	18.71	−30.575	1	23.6	O
ATOM	2218	NE2	GLN B	112	−12.395	18.088	−28.886	1	27.09	N
ATOM	2219	H	GLN B	112	−6.775	16.136	−30.133	1	19.65	H
ATOM	2220	HA	GLN B	112	−9.152	17.21	−30.842	1	22.24	H
ATOM	2221	HB2	GLN B	112	−9.601	16.285	−28.751	1	21.98	H
ATOM	2222	HB3	GLN B	112	−8.38	17.085	−28.13	1	21.98	H
ATOM	2223	HG2	GLN B	112	−10.359	18.142	−27.559	1	24.51	H
ATOM	2224	HG3	GLN B	112	−9.517	19.096	−28.511	1	24.51	H
ATOM	2225	HE21	GLN B	112	−13.099	18.134	−29.378	1	32.51	H
ATOM	2226	HE22	GLN B	112	−12.462	17.858	−28.06	1	32.51	H
ATOM	2227	N	PHE B	113	−8.309	19.484	−30.923	1	17.31	N
ATOM	2228	CA	PHE B	113	−7.731	20.801	−31.141	1	18.02	C
ATOM	2229	C	PHE B	113	−8.352	21.798	−30.178	1	19.91	C
ATOM	2230	O	PHE B	113	−9.508	22.181	−30.346	1	25.64	O
ATOM	2231	CB	PHE B	113	−7.961	21.259	−32.583	1	16.63	C
ATOM	2232	CG	PHE B	113	−7.265	20.414	−33.612	1	20.32	C
ATOM	2233	CD1	PHE B	113	−7.73	19.144	−33.92	1	23.5	C
ATOM	2234	CD2	PHE B	113	−6.158	20.898	−34.285	1	20.35	C
ATOM	2235	CE1	PHE B	113	7.092	18.371	−34.87	1	25.58	C
ATOM	2236	CE2	PHE B	113	−5.515	20.128	−35.235	1	24.89	C
ATOM	2237	CZ	PHE B	113	−5.984	18.863	−35.529	1	28.96	C
ATOM	2238	H	PHE B	113	−9.11	19.41	−31.227	1	20.77	H
ATOM	2239	HA	PHE B	113	−6.775	20.767	−30.977	1	21.62	H
ATOM	2240	HB2	PHE B	113	8.913	21.23	−32.77	1	19.95	H
ATOM	2241	HB3	PHE B	113	−7.636	22.168	−32.677	1	19.95	H
ATOM	2242	HD1	PHE B	113	−8.475	18.807	−33.478	1	28.2	H
ATOM	2243	HD2	PHE B	113	−5.837	21.749	−34.09	1	24.42	H
ATOM	2244	HE1	PHE B	113	−7.41	17.519	−35.066	1	30.7	H
ATOM	2245	HE2	PHE B	113	−4.769	20.463	−35.678	1	29.86	H
ATOM	2246	HZ	PHE B	113	−5.554	18.344	−36.17	1	34.75	H
ATOM	2247	N	PHE B	114	−7.589	22.215	−29.173	1	18.14	N
ATOM	2248	CA	PHE B	114	−8.09	23.146	−28.167	1	16.48	C
ATOM	2249	C	PHE B	114	−7.775	24.587	−28.554	1	19.56	C
ATOM	2250	O	PHE B	114	−6.611	24.962	−28.675	1	18.71	O
ATOM	2251	CB	PHE B	114	−7.496	22.821	−26.799	1	19.55	C
ATOM	2252	CG	PHE B	114	−7.961	21.508	−26.237	1	21.13	C
ATOM	2253	CD1	PHE B	114	−7.233	20.352	−26.45	1	21.85	C
ATOM	2254	CD2	PHE B	114	−9.132	21.429	−25.501	1	27.16	C
ATOM	2255	CE1	PHE B	114	−7.658	19.14	−25.935	1	21.25	C
ATOM	2256	CE2	PHE B	114	−9.564	20.218	−24.984	1	27.33	C
ATOM	2257	CZ	PHE B	114	−8.824	19.074	−25.202	1	22.66	C
ATOM	2258	H	PHE B	114	−6.773	21.972	−29.05	1	21.76	H
ATOM	2259	HA	PHE B	114	−9.054	23.056	−28.105	1	19.78	H
ATOM	2260	HB2	PHE B	114	−6.53	22.785	−26.878	1	23.47	H
ATOM	2261	HB3	PHE B	114	−7.75	23.518	−26.174	1	23.47	H
ATOM	2262	HD1	PHE B	114	−6.445	20.391	−26.942	1	26.22	H
ATOM	2263	HD2	PHE B	114	−9.633	22.198	−25.351	1	32.6	H
ATOM	2264	HE1	PHE B	114	−7.158	18.37	−26.084	1	25.5	H
ATOM	2265	HE2	PHE B	114	−10.351	20.176	−24.49	1	32.79	H
ATOM	2266	HZ	PHE B	114	−9.111	18.26	−24.856	1	27.2	H
ATOM	2267	N	ASP B	115	−8.82	25.391	−28.738	1	19.34	N
ATOM	2268	CA	ASP B	115	−8.666	26.759	−29.234	1	22.18	C
ATOM	2269	C	ASP B	115	−8.421	27.778	−28.121	1	22.24	C
ATOM	2270	O	ASP B	115	−8.374	28.983	−28.375	1	23.21	O
ATOM	2271	CB	ASP B	115	−9.896	27.172	−30.053	1	28.95	C
ATOM	2272	CG	ASP B	115	−11.204	26.959	−29.31	1	30.69	C
ATOM	2273	OD1	ASP B	115	−11.201	26.953	−28.06	1	36.27	O
ATOM	2274	OD2	ASP B	115	−12.244	26.8	−29.985	1	43.5	O1−
ATOM	2275	H	ASP B	115	−9.636	25.167	−28.582	1	23.21	H
ATOM	2276	HA	ASP B	115	−7.898	26.786	−29.826	1	26.62	H
ATOM	2277	HB2	ASP B	115	9.827	28.115	−30.272	1	34.74	H
ATOM	2278	HB3	ASP B	115	−9.925	26.645	−30.866	1	34.74	H
ATOM	2279	N	GLU B	116	−8.267	27.295	−26.892	1	21.76	N
ATOM	2280	CA	GLU B	116	−7.861	28.151	−25.782	1	25.37	C
ATOM	2281	C	GLU B	116	−6.344	28.309	−25.771	1	26.04	C
ATOM	2282	0	GLU B	116	−5.61	27.323	−25.778	1	26.31	O
ATOM	2283	CB	GLU B	116	−8.34	27.578	−24.447	1	30.28	C
ATOM	2284	CG	GLU B	116	−9.811	27.839	−24.153	1	43.86	C
ATOM	2285	CD	GLU B	116	−10.256	27.25	−22.827	1	59.8	C
ATOM	2286	OE1	GLU B	116	−9.383	26.828	−22.037	1	55.77	O
ATOM	2287	OE2	GLU B	116	−11.48	27.208	−22.576	1	69.76	O1−
ATOM	2288	H	GLU B	116	−8.391	26.473	−26.674	1	26.11	H
ATOM	2289	HA	GLU B	116	−8.256	29.029	−25.895	1	30.45	H
ATOM	2290	HB2	GLU B	116	−8.205	26.618	−24.453	1	36.34	H
ATOM	2291	HB3	GLU B	116	−7.82	27.978	−23.732	1	36.34	H
ATOM	2292	HG2	GLU B	116	−9.963	28.796	−24.123	1	52.63	H
ATOM	2293	HG3	GLU B	116	−10.349	27.439	−24.855	1	52.63	H
ATOM	2294	N	SER B	117	−5.878	29.551	−25.757	1	24.25	N
ATOM	2295	CA	SER B	117	−4.446	29.825	−25.766	1	24.22	C
ATOM	2296	C	SER B	117	−3.832	29.548	−24.401	1	24.91	C
ATOM	2297	0	SER B	117	−4.271	30.095	−23.39	1	25.88	O
ATOM	2298	CB	SER B	117	−4.179	31.275	−26.178	1	25.72	C
ATOM	2299	OG	SER B	117	−4.568	31.501	−27.519	1	35.43	O
ATOM	2300	H	SER B	117	−6.371	30.256	−25.743	1	29.1	H
ATOM	2301	HA	SER B	117	−4.017	29.244	−26.413	1	29.07	H
ATOM	2302	HB2	SER B	117	−4.687	31.865	−25.599	1	30.86	H
ATOM	2303	HB3	SER B	117	−3.231	31.458	−26.089	1	30.86	H
ATOM	2304	HG	SER B	117	−4.416	32.299	−27.731	1	42.52	H
ATOM	2305	N	LYS B	118	−2.815	28.692	−24.384	1	17.66	N
ATOM	2306	CA	LYS B	118	−2.093	28.355	−23.163	1	23.06	C
ATOM	2307	C	LYS B	118	−0.612	28.252	−23.478	1	21.34	C
ATOM	2308	O	LYS B	118	−0.238	27.982	−24.623	1	18.83	O
ATOM	2309	CB	LYS B	118	−2.597	27.035	−22.571	1	22.84	C
ATOM	2310	CG	LYS B	118	−4.06	27.046	−22.162	1	24.02	C
ATOM	2311	CD	LYS B	118	−4.473	25.704	−21.567	1	26.42	C
ATOM	2312	CE	LYS B	118	−5.958	25.669	−21.232	1	32.25	C
ATOM	2313	NZ	LYS B	118	−6.343	26.77	−20.307	1	35.19	N1+
ATOM	2314	H	LYS B	118	−2.518	28.286	−25.082	1	21.19	H
ATOM	2315	HA	LYS B	118	−2.222	29.057	−22.506	1	27.68	H
ATOM	2316	HB2	LYS B	118	−2.481	26.335	−23.231	1	27.41	H
ATOM	2317	HB3	LYS B	118	−2.072	26.83	−21.781	1	27.41	H
ATOM	2318	HG2	LYS B	118	−4.202	27.733	−21.492	1	28.83	H
ATOM	2319	HG3	LYS B	118	−4.611	27.216	−22.942	1	28.83	H
ATOM	2320	HD2	LYS B	118	−4.29	25	−22.209	1	31.7	H
ATOM	2321	HD3	LYS B	118	−3.974	25.55	−20.749	1	31.7	H
ATOM	2322	HE2	LYS B	118	−6.471	25.767	−22.049	1	38.7	H
ATOM	2323	HE3	LYS B	118	−6.168	24.825	−20.803	1	38.7	H
ATOM	2324	HZ1	LYS B	118	−5.888	26.7	−19.545	1	42.23	H
ATOM	2325	HZ2	LYS B	118	−6.164	27.557	−20.68	1	42.23	H
ATOM	2326	HZ3	LYS B	118	−7.214	26.726	−20.129	1	42.23	H
ATOM	2327	N	ASN B	119	0.236	28.473	−22.478	1	16.27	N
ATOM	2328	CA	ASN B	119	1.659	28.241	−22.668	1	20.3	C
ATOM	2329	C	ASN B	119	1.878	26.738	−22.763	1	16.48	C
ATOM	2330	O	ASN B	119	0.946	25.951	−22.569	1	17.62	O
ATOM	2331	CB	ASN B	119	2.499	28.869	−21.542	1	19.64	C
ATOM	2332	CG	ASN B	119	2.262	28.228	−20.183	1	20.65	C
ATOM	2333	OD1	ASN B	119	2.498	27.035	−19.986	1	17.21	O
ATOM	2334	ND2	ASN B	119	1.823	29.036	−19.224	1	20.04	N
ATOM	2335	H	ASN B	119	0.016	28.753	−21.695	1	19.52	H
ATOM	2336	HA	ASN B	119	1.936	28.639	−23.508	1	24.36	H
ATOM	2337	HB2	ASN B	119	3.439	28.769	−21.759	1	23.57	H
ATOM	2338	HB3	ASN B	119	2.275	29.81	−21.471	1	23.57	H
ATOM	2339	HD21	ASN B	119	1.673	28.726	−18.436	1	24.05	H
ATOM	2340	HD22	ASN B	119	1.691	29.869	−19.391	1	24.05	H
ATOM	2341	N	TRP B	120	3.102	26.333	−23.067	1	15.24	N
ATOM	2342	CA	TRP B	120	3.362	24.93	−23.348	1	16.04	C
ATOM	2343	C	TRP B	120	3.052	24.039	−22.148	1	19.13	C
ATOM	2344	O	TRP B	120	2.588	22.909	−22.313	1	15.63	O
ATOM	2345	CB	TRP B	120	4.813	24.733	−23.779	1	16.87	C
ATOM	2346	CG	TRP B	120	5.085	23.34	−24.242	1	15.71	C
ATOM	2347	CD1	TRP B	120	5.006	22.874	−25.52	1	15.03	C
ATOM	2348	CD2	TRP B	120	5.465	22.226	−23.431	1	19.26	C
ATOM	2349	NE1	TRP B	120	5.318	21.54	−25.558	1	16.56	N
ATOM	2350	CE2	TRP B	120	5.604	21.116	−24.288	1	19.91	C
ATOM	2351	CE3	TRP B	120	5.703	22.059	−22.064	1	20.14	C
ATOM	2352	CZ2	TRP B	120	5.972	19.856	−23.823	1	20.45	C
ATOM	2353	CZ3	TRP B	120	6.068	20.807	−21.604	1	24	C
ATOM	2354	CH2	TRP B	120	6.199	19.721	−22.482	1	20.1	C
ATOM	2355	H	TRP B	120	3.792	26.844	−23.117	1	18.29	H
ATOM	2356	HA	TRP B	120	2.793	24.648	−24.082	1	19.25	H
ATOM	2357	HB2	TRP B	120	5.012	25.338	−24.51	1	20.25	H
ATOM	2358	HB3	TRP B	120	5.395	24.918	−23.025	1	20.25	H
ATOM	2359	HD1	TRP B	120	4.775	23.387	−26.261	1	18.03	H
ATOM	2360	HE1	TRP B	120	5.332	21.049	−26.264	1	19.88	H
ATOM	2361	HE3	TRP B	120	5.618	22.775	−21.476	1	24.16	H
ATOM	2362	HZ2	TRP B	120	6.06	19.134	−24.403	1	24.54	H
ATOM	2363	HZ3	TRP B	120	6.23	20.683	−20.697	1	28.8	H
ATOM	2364	HH2	TRP B	120	6.446	18.891	−22.144	1	24.12	H
ATOM	2365	N	TYR B	121	3.297	24.553	−20.946	1	20.9	N
ATOM	2366	CA	TYR B	121	3.179	23.75	−19.733	1	19.53	C
ATOM	2367	C	TYR B	121	1.735	23.563	−19.268	1	17.33	C
ATOM	2368	O	TYR B	121	1.386	22.498	−18.763	1	20.12	O
ATOM	2369	CB	TYR B	121	4.006	24.375	−18.612	1	20.76	C
ATOM	2370	CG	TYR B	121	5.479	24.438	−18.945	1	27.57	C
ATOM	2371	CD1	TYR B	121	6.266	23.294	−18.909	1	26.72	C
ATOM	2372	CD2	TYR B	121	6.077	25.635	−19.312	1	22	C
ATOM	2373	CE1	TYR B	121	7.607	23.343	−19.222	1	27.02	C
ATOM	2374	CE2	TYR B	121	7.416	25.693	−19.623	1	29.21	C
ATOM	2375	CZ	TYR B	121	8.175	24.544	−19.578	1	30.61	C
ATOM	2376	OH	TYR B	121	9.511	24.599	−19.891	1	42.9	O
ATOM	2377	H	TYR B	121	3.533	25.368	−20.805	1	25.08	H
ATOM	2378	HA	TYR B	121	3.545	22.869	−19.911	1	23.43	H
ATOM	2379	HB2	TYR B	121	3.694	25.28	−18.455	1	24.91	H
ATOM	2380	HB3	TYR B	121	3.902	23.843	−17.807	1	24.91	H
ATOM	2381	HD1	TYR B	121	5.882	22.481	−18.67	1	32.06	H
ATOM	2382	HD2	TYR B	121	5.565	26.411	−19.344	1	26.41	H
ATOM	2383	HE1	TYR B	121	8.124	22.57	−19.192	1	32.42	H
ATOM	2384	HE2	TYR B	121	7.805	26.502	−19.866	1	35.05	H
ATOM	2385	HH	TYR B	121	9.728	25.386	−20.088	1	51.48	H
ATOM	2386	N	GLU B	122	0.899	24.586	−19.418	1	19.17	N
ATOM	2387	CA	GLU B	122	−0.514	24.422	−19.074	1	20.84	C
ATOM	2388	C	GLU B	122	−1.187	23.598	−20.161	1	20.4	C
ATOM	2389	0	GLU B	122	−2.164	22.904	−19.895	1	23.74	O
ATOM	2390	CB	GLU B	122	−1.24	25.765	−18.887	1	25.11	C
ATOM	2391	CG	GLU B	122	−0.55	26.974	−19.475	1	30.11	C
ATOM	2392	CD	GLU B	122	−1.378	28.248	−19.377	1	32.89	C
ATOM	2393	OE1	GLU B	122	−2.424	28.235	−18.687	1	36.08	O
ATOM	2394	OE2	GLU B	122	−0.975	29.264	−19.988	1	26.01	O1−
ATOM	2395	H	GLU B	122	1.114	25.366	−19.709	1	23.01	H
ATOM	2396	HA	GLU B	122	−0.58	23.929	−18.241	1	25	H
ATOM	2397	HB2	GLU B	122	−2.114	25.699	−19.303	1	30.13	H
ATOM	2398	HB3	GLU B	122	−1.346	25.925	−17.937	1	30.13	H
ATOM	2399	HG2	GLU B	122	0.283	27.123	−19	1	36.13	H
ATOM	2400	HG3	GLU B	122	−0.369	26.807	−20.414	1	36.13	H
ATOM	2401	N	SER B	123	−0.657	23.676	−21.382	1	17.88	N
ATOM	2402	CA	SER B	123	−1.132	22.838	−22.477	1	18.47	C
ATOM	2403	C	SER B	123	−0.844	21.374	−22.16	1	17.37	C
ATOM	2404	0	SER B	123	−1.706	20.515	−22.321	1	17.15	O
ATOM	2405	CB	SER B	123	−0.472	23.23	−23.805	1	17.79	C
ATOM	2406	OG	SER B	123	−0.916	24.501	−24.251	1	16.72	O
ATOM	2407	H	SER B	123	−0.019	24.209	−21.6	1	21.45	H
ATOM	2408	HA	SER B	123	−2.091	22.946	−22.571	1	22.17	H
ATOM	2409	HB2	SER B	123	0.49	23.261	−23.68	1	21.34	H
ATOM	2410	HB3	SER B	123	−0.697	22.567	−24.475	1	21.34	H
ATOM	2411	HG	SER B	123	−0.727	25.088	−23.681	1	20.06	H
ATOM	2412	N	GLN B	124	0.376	21.105	−21.709	1	17.12	N
ATOM	2413	CA	GLN B	124	0.765	19.765	−21.286	1	19.26	C
ATOM	2414	C	GLN B	124	−0.119	19.251	−20.156	1	17.95	C
ATOM	2415	O	GLN B	124	−0.516	18.086	−20.153	1	18.47	O
ATOM	2416	CB	GLN B	124	2.225	19.751	−20.831	1	19.97	C
ATOM	2417	CG	GLN B	124	2.631	18.463	−20.125	1	20.4	C
ATOM	2418	CD	GLN B	124	4.098	18.437	−19.763	1	25.03	C
ATOM	2419	OE1	GLN B	124	4.522	19.09	−18.811	1	29	O
ATOM	2420	NE2	GLN B	124	4.884	17.686	−20.523	1	22.34	N
ATOM	2421	H	GLN B	124	1.004	21.688	−21.639	1	20.54	H
ATOM	2422	HA	GLN B	124	0.678	19.158	−22.037	1	23.11	H
ATOM	2423	HB2	GLN B	124	2.797	19.856	−21.607	1	23.97	H
ATOM	2424	HB3	GLN B	124	2.369	20.485	−20.214	1	23.97	H
ATOM	2425	HG2	GLN B	124	2.118	18.376	−19.307	1	24.48	H
ATOM	2426	HG3	GLN B	124	2.452	17.711	−20.711	1	24.48	H
ATOM	2427	HE21	GLN B	124	5.726	17.639	−20.356	1	26.81	H
ATOM	2428	HE22	GLN B	124	4.551	17.246	−21.183	1	26.81	H
ATOM	2429	N	ALA B	125	−0.397	20.118	−19.186	1	19.16	N
ATOM	2430	CA	ALA B	125	−1.234	19.754	−18.05	1	21.66	C
ATOM	2431	C	ALA B	125	−2.65	19.437	−18.513	1	22.92	C
ATOM	2432	O	ALA B	125	−3.292	18.528	−17.996	1	22.29	O
ATOM	2433	CB	ALA B	125	−1.251	20.873	−17.021	1	21.65	C
ATOM	2434	H	ALA B	125	−0.111	20.928	−19.164	1	23	H
ATOM	2435	HA	ALA B	125	−0.87	18.961	−17.627	1	26	H
ATOM	2436	HB1	ALA B	125	−1.813	20.609	−16.276	1	25.98	H
ATOM	2437	HB2	ALA B	125	−0.345	21.032	−16.712	1	25.98	H
ATOM	2438	HB3	ALA B	125	−1.605	21.676	−17.434	1	25.98	H
ATOM	2439	N	SER B	126	−3.129	20.199	−19.491	1	19.48	N
ATOM	2440	CA	SER B	126	−4.467	20.008	−20.035	1	22.96	C
ATOM	2441	C	SER B	126	−4.622	18.638	−20.696	1	24.3	C
ATOM	2442	O	SER B	126	−5.617	17.945	−20.474	1	23.17	O
ATOM	2443	CB	SER B	126	−4.79	21.113	−21.042	1	21.51	C
ATOM	2444	OG	SER B	126	−6.033	20.874	−21.679	1	26.37	O
ATOM	2445	H	SER B	126	−2.692	20.841	−19.861	1	23.37	H
ATOM	2446	HA	SER B	126	−5.111	20.065	−19.311	1	27.56	H
ATOM	2447	HB2	SER B	126	−4.833	21.962	−20.575	1	25.81	H
ATOM	2448	HB3	SER B	126	−4.091	21.14	−21.714	1	25.81	H
ATOM	2449	HG	SER B	126	−6.197	21.488	−22.228	1	31.64	H
ATOM	2450	N	CYS B	127	−3.646	18.251	−21.511	1	19.38	N
ATOM	2451	CA	CYS B	127	−3.696	16.956	−22.182	1	17.72	C
ATOM	2452	C	CYS B	127	−3.596	15.833	−21.158	1	23.86	C
ATOM	2453	O	CYS B	127	−4.292	14.824	−21.262	1	24.87	O
ATOM	2454	CB	CYS B	127	−2.574	16.829	−23.215	1	16.67	C
ATOM	2455	SG	CYS B	127	−2.664	18.028	−24.573	1	18.01	S
ATOM	2456	H	CYS B	127	−2.946	18.717	−21.692	1	23.26	H
ATOM	2457	HA	CYS B	127	−4.544	16.869	−22.644	1	21.26	H
ATOM	2458	HB2	CYS B	127	−1.724	16.956	−22.766	1	20.01	H
ATOM	2459	HB3	CYS B	127	−2.61	15.941	−23.603	1	20.01	H
ATOM	2460	N	MET B	128	−2.728	16.014	−20.169	1	21.99	N
ATOM	2461	CA	MET B	128	−2.562	15.018	−19.119	1	30.3	C
ATOM	2462	C	MET B	128	−3.878	14.767	−18.387	1	27.68	C
ATOM	2463	O	MET B	128	−4.261	13.62	−18.166	1	33.94	O
ATOM	2464	CB	MET B	128	−1.491	15.452	−18.115	1	27.2	C
ATOM	2465	CG	MET B	128	−1.259	14.418	−17.019	1	33.45	C
ATOM	2466	SD	MET B	128	0.009	14.851	−15.796	1	47.54	S
ATOM	2467	CE	MET B	128	−0.094	13.355	−14.801	1	39.77	C
ATOM	2468	H	MET B	128	−2.224	16.706	−20.083	1	26.39	H
ATOM	2469	HA	MET B	128	−2.267	14.187	−19.523	1	36.36	H
ATOM	2470	HB2	MET B	128	−0.652	15.585	−18.584	1	32.64	H
ATOM	2471	HB3	MET B	128	−1.77	16.279	−17.692	1	32.64	H
ATOM	2472	HG2	MET B	128	−2.094	14.281	−16.545	1	40.14	H
ATOM	2473	HG3	MET B	128	−0.983	13.587	−17.435	1	40.14	H
ATOM	2474	HE1	MET B	128	−0.994	13.26	−14.451	1	47.73	H
ATOM	2475	HE2	MET B	128	0.126	12.593	−15.359	1	47.73	H
ATOM	2476	HE3	MET B	128	0.54	13.426	−14.071	1	47.73	H
ATOM	2477	N	SER B	129	−4.573	15.842	−18.029	1	29.26	N
ATOM	2478	CA	SER B	129	−5.795	15.737	−17.233	1	32.8	C
ATOM	2479	C	SER B	129	−6.901	14.984	−17.968	1	29.82	C
ATOM	2480	0	SER B	129	−7.932	14.658	−17.381	1	30.42	O
ATOM	2481	CB	SER B	129	−6.296	17.127	−16.839	1	32.72	C
ATOM	2482	OG	SER B	129	−6.872	17.799	−17.945	1	38.37	O
ATOM	2483	H	SER B	129	−4.358	16.649	−18.235	1	35.11	H
ATOM	2484	HA	SER B	129	−5.596	15.25	−16.418	1	39.36	H
ATOM	2485	HB2	SER B	129	−6.966	17.034	−16.144	1	39.26	H
ATOM	2486	HB3	SER B	129	−5.548	17.649	−16.509	1	39.26	H
ATOM	2487	HG	SER B	129	−6.302	17.888	−18.556	1	46.05	H
ATOM	2488	N	GLN B	130	−6.682	14.717	−19.251	1	32.61	N
ATOM	2489	CA	GLN B	130	−7.63	13.962	−20.059	1	32.51	C
ATOM	2490	C	GLN B	130	−7.007	12.648	−20.517	1	30.71	C
ATOM	2491	0	GLN B	130	−7.402	12.083	−21.536	1	31.54	O
ATOM	2492	CB	GLN B	130	−8.082	14.801	−21.255	1	34.47	C
ATOM	2493	CG	GLN B	130	−8.648	16.155	−20.845	1	35.04	C
ATOM	2494	CD	GLN B	130	−8.999	17.038	−22.023	1	35.73	C
ATOM	2495	OE1	GLN B	130	−9.762	16.647	−22.906	1	32.33	O
ATOM	2496	NE2	GLN B	130	−8.442	18.245	−22.04	1	42.1	N
ATOM	2497	H	GLN B	130	−5.981	14.966	−19.681	1	39.14	H
ATOM	2498	HA	GLN B	130	−8.411	13.755	−19.523	1	39.01	H
ATOM	2499	HB2	GLN B	130	−7.322	14.957	−21.837	1	41.37	H
ATOM	2500	HB3	GLN B	130	−8.774	14.319	−21.735	1	41.37	H
ATOM	2501	HG2	GLN B	130	−9.456	16.015	−20.327	1	42.05	H
ATOM	2502	HG3	GLN B	130	−7.988	16.622	−20.309	1	42.05	H
ATOM	2503	HE21	GLN B	130	−8.608	18.786	−22.687	1	50.53	H
ATOM	2504	HE22	GLN B	130	−7.915	18.484	−21.404	1	50.53	H
ATOM	2505	N	ASN B	131	−6.032	12.168	−19.75	1	31.89	N
ATOM	2506	CA	ASN B	131	−5.372	10.896	−20.028	1	35.86	C
ATOM	2507	C	ASN B	131	−4.77	10.869	−21.431	1	35.32	C
ATOM	2508	0	ASN B	131	4.818	9.852	−22.125	1	31.56	O
ATOM	2509	CB	ASN B	131	−6.358	9.74	−19.852	1	44.38	C
ATOM	2510	CG	ASN B	131	−5.665	8.403	−19.679	1	65.46	C
ATOM	2511	OD1	ASN B	131	−5.153	8.093	−18.604	1	82.44	O
ATOM	2512	ND2	ASN B	131	−5.648	7.603	−20.737	1	73.37	N
ATOM	2513	H	ASN B	131	−5.73	12.567	−19.05	1	38.26	H
ATOM	2514	HA	ASN B	131	−4.65	10.772	−19.392	1	43.03	H
ATOM	2515	HB2	ASN B	131	−6.899	9.903	−19.063	1	53.26	H
ATOM	2516	HB3	ASN B	131	−6.925	9.685	−20.638	1	53.26	H
ATOM	2517	HD21	ASN B	131	−5.267	6.833	−20.689	1	88.04	H
ATOM	2518	HD22	ASN B	131	−6.019	7.853	−21.472	1	88.04	H
ATOM	2519	N	ALA B	132	−4.206	12.001	−21.838	1	25.52	N
ATOM	2520	C	ALA B	132	−3.593	12.132	−23.153	1	27.44	C
ATOM	2521	C	ALA B	132	−2.264	12.868	−23.05	1	26.46	C
ATOM	2522	0	ALA B	132	−1.802	13.178	−21.954	1	24.84	O
ATOM	2523	CB	ALA B	132	−4.533	12.86	−24.1	1	24.28	C
ATOM	2524	H	ALA B	132	−4.166	12.717	−21.364	1	30.62	H
ATOM	2525	HA	ALA B	132	−3.422	11.248	−23.515	1	32.93	H
ATOM	2526	HB1	ALA B	132	−4.107	12.937	−24.969	1	29.14	H
ATOM	2527	HB2	ALA B	132	−5.356	12.353	−24.179	1	29.14	H
ATOM	2528	HB3	ALA B	132	−4.719	13.742	−23.743	1	29.14	H
ATOM	2529	N	SER B	133	−1.657	13.137	−24.201	1	21.19	N
ATOM	2530	CA	SER B	133	−0.426	13.913	−24.27	1	20.84	C
ATOM	2531	C	SER B	133	−0.54	14.942	−25.383	1	21.2	C
ATOM	2532	0	SER B	133	−1.48	14.903	−26.177	1	19.82	O
ATOM	2533	CB	SER B	133	0.776	13.001	−24.514	1	26.77	C
ATOM	2534	OG	SER B	133	0.841	11.979	−23.535	1	32.82	O
ATOM	2535	H	SER B	133	−1.944	12.875	−24.968	1	25.43	H
ATOM	2536	HA	SER B	133	−0.292	14.381	−23.431	1	25.01	H
ATOM	2537	HB2	SER B	133	0.691	12.594	−25.39	1	32.13	H
ATOM	2538	HB3	SER B	133	1.588	13.53	−24.472	1	32.13	H
ATOM	2539	HG	SER B	133	0.914	12.318	−22.77	1	39.39	H
ATOM	2540	N	LEU B	134	0.404	15.873	−25.431	1	18.46	N
ATOM	2541	CA	LEU B	134	0.479	16.796	−26.55	1	18.04	C
ATOM	2542	C	LEU B	134	0.794	15.995	−27.806	1	21	C
ATOM	2543	O	LEU B	134	1.303	14.877	−27.723	1	18.42	O
ATOM	2544	CB	LEU B	134	1.54	17.869	−26.311	1	20.17	C
ATOM	2545	CG	LEU B	134	1.167	18.973	−25.319	1	19.25	C
ATOM	2546	CD1	LEU B	134	2.4	19.78	−24.937	1	19.48	C
ATOM	2547	CD2	LEU B	134	0.096	19.889	−25.898	1	16.17	C
ATOM	2548	H	LEU B	134	1.01	15.99	−24.831	1	22.15	H
ATOM	2549	HA	LEU B	134	−0.379	17.231	−26.669	1	21.65	H
ATOM	2550	HB2	LEU B	134	2.341	17.437	−25.976	1	24.2	H
ATOM	2551	HB3	LEU B	134	1.736	18.298	−27.159	1	24.2	H
ATOM	2552	HG	LEU B	134	0.812	18.567	−24.513	1	23.1	H
ATOM	2553	HD11	LEU B	134	2.142	20.472	−24.308	1	23.37	H
ATOM	2554	HD12	LEU B	134	3.05	19.187	−24.528	1	23.37	H
ATOM	2555	HD13	LEU B	134	2.775	20.181	−25.736	1	23.37	H
ATOM	2556	HD21	LEU B	134	−0.117	20.576	−25.247	1	19.4	H
ATOM	2557	HD22	LEU B	134	0.435	20.297	−26.71	1	19.4	H
ATOM	2558	HD23	LEU B	134	−0.695	19.363	−26.097	1	19.4	H
ATOM	2559	N	LEU B	135	0.486	16.57	−28.963	1	15.7	N
ATOM	2560	CA	LEU B	135	0.693	15.894	−30.236	1	15.71	C
ATOM	2561	C	LEU B	135	2.099	15.32	−30.37	1	16.68	C
ATOM	2562	O	LEU B	135	3.084	16.02	−30.142	1	15.25	O
ATOM	2563	CB	LEU B	135	0.43	16.862	−31.388	1	13.32	C
ATOM	2564	CG	LEU B	135	0.715	16.342	−32.793	1	13.52	C
ATOM	2565	CD1	LEU B	135	−0.22	15.193	−33.142	1	16.61	C
ATOM	2566	CD2	LEU B	135	0.582	17.468	−33.796	1	13.74	C
ATOM	2567	H	LEU B	135	0.152	17.359	−29.037	1	18.84	H
ATOM	2568	HA	LEU B	135	0.062	15.161	−30.31	1	18.85	H
ATOM	2569	HB2	LEU B	135	−0.505	17.12	−31.36	1	15.99	H
ATOM	2570	HB3	LEU B	135	0.983	17.648	−31.255	1	15.99	H
ATOM	2571	HG	LEU B	135	1.626	16.011	−32.831	1	16.22	H
ATOM	2572	HD11	LEU B	135	−0.017	14.882	−34.038	1	19.93	H
ATOM	2573	HD12	LEU B	135	−0.087	14.474	−32.504	1	19.93	H
ATOM	2574	HD13	LEU B	135	−1.136	15.508	−33.099	1	19.93	H
ATOM	2575	HD21	LEU B	135	0.765	17.123	−34.684	1	16.49	H
ATOM	2576	HD22	LEU B	135	−0.321	17.82	−33.758	1	16.49	H
ATOM	2577	HD23	LEU B	135	1.219	18.165	−33.574	1	16.49	H
ATOM	2578	N	LYS B	136	2.178	14.042	−30.735	1	16.35	N
ATOM	2579	CA	LYS B	136	3.437	13.426	−31.139	1	16.55	C
ATOM	2580	C	LYS B	136	3.381	13.084	−32.624	1	17.63	C
ATOM	2581	O	LYS B	136	2.532	12.309	−33.055	1	21.03	O
ATOM	2582	CB	LYS B	136	3.728	12.163	−30.323	1	19.4	C
ATOM	2583	CG	LYS B	136	4.973	11.413	−30.793	1	19.92	C
ATOM	2584	CD	LYS B	136	5.2	10.114	−30.027	1	27.62	C
ATOM	2585	CE	LYS B		136	6.484	9.429	−30.494	1	26.76	C
ATOM	2586	NZ	LYS B	136	6.768	8.164	−29.765	1	29.82	N1+
ATOM	2587	H	LYS B	136	1.507	13.505	−30.757	1	19.62	H
ATOM	2588	HA	LYS B	136	4.162	14.054	−30.998	1	19.86	H
ATOM	2589	HB2	LYS B	136	3.863	12.413	−29.395	1	23.28	H
ATOM	2590	HB3	LYS B	136	2.972	11.56	−30.396	1	23.28	H
ATOM	2591	HG2	LYS B	136	4.875	11.194	−31.733	1	23.9	H
ATOM	2592	HG3	LYS B	136	5.751	11.978	−30.663	1	23.9	H
ATOM	2593	HD2	LYS B	136	5.283	10.307	−29.08	1	33.15	H
ATOM	2594	HD3	LYS B	136	4.457	9.511	−30.186	1	33.15	H
ATOM	2595	HE2	LYS B	136	6.403	9.219	−31.437	1	32.11	H
ATOM	2596	HE3	LYS B	136	7.231	10.031	−30.351	1	32.11	H
ATOM	2597	HZ1	LYS B	136	6.101	7.588	−29.885	1	35.78	H
ATOM	2598	HZ2	LYS B	136	7.522	7.802	−30.069	1	35.78	H
ATOM	2599	HZ3	LYS B	136	6.856	8.328	−28.895	1	35.78	H
ATOM	2600	N	VAL B	137	4.281	13.676	−33.401	1	17.2	N
ATOM	2601	CA	VAL B	137	4.399	13.367	−34.822	1	17.92	C
ATOM	2602	C	VAL B	137	5.388	12.221	−34.998	1	22.09	C
ATOM	2603	O	VAL B	137	6.556	12.346	−34.63	1	20.93	O
ATOM	2604	CB	VAL B	137	4.868	14.59	−35.643	1	23.08	C
ATOM	2605	CG1	VAL B	137	5.015	14.234	−37.124	1	22.11	C
ATOM	2606	CG2	VAL B	137	3.896	15.744	−35.477	1	15.93	C
ATOM	2607	H	VAL B		137	4.842	14.268	−33.126	1	20.64	H
ATOM	2608	HA	VAL B	137	3.537	13.082	−35.162	1	21.51	H
ATOM	2609	HB	VAL B	137	5.734	14.878	−35.316	1	27.69	H
ATOM	2610	HG11	VAL B	137	5.309	15.02	−37.61	1	26.53	H
ATOM	2611	HG12	VAL B	137	5.67	13.525	−37.214	1	26.53	H
ATOM	2612	HG13	VAL B	137	4.156	13.937	−37.464	1	26.53	H
ATOM	2613	HG21	VAL B	137	4.21	16.499	−36	1	19.12	H
ATOM	2614	HG22	VAL B	137	3.021	15.467	−35.789	1	19.12	H
ATOM	2615	HG23	VAL B	137	3.852	15.987	−34.539	1	19.12	H
ATOM	2616	N	TYR B	138	4.915	11.113	−35.563	1	20.52	N
ATOM	2617	CA	TYR B	138	5.748	9.928	−35.754	1	25.3	C
ATOM	2618	C	TYR B	138	5.614	9.342	−37.163	1	26.25	C
ATOM	2619	O	TYR B	138	6.481	8.587	−37.601	1	27.44	O
ATOM	2620	CB	TYR B	138	5.393	8.861	−34.713	1	26.97	C
ATOM	2621	CG	TYR B	138	4.047	8.217	−34.94	1	23.68	C
ATOM	2622	CD1	TYR B	138	2.886	8.797	−34.451	1	23.08	C
ATOM	2623	CD2	TYR B	138	3.938	7.028	−35.65	1	27.12	C
ATOM	2624	CE1	TYR B	138	1.654	8.212	−34.661	1	25.34	C
ATOM	2625	CE2	TYR B	138	2.709	6.437	−35.867	1	26.65	C
ATOM	2626	CZ	TYR B	138	1.572	7.033	−35.371	1	28.22	C
ATOM	2627	OH	TYR B	138	0.347	6.447	−35.581	1	30.35	O
ATOM	2628	H	TYR B	138	4.108	11.021	−35.847	1	24.63	H
ATOM	2629	HA	TYR B	138	6.676	10.175	−35.623	1	30.36	H
ATOM	2630	HB2	TYR B	138	6.066	8.163	−34.74	1	32.36	H
ATOM	2631	HB3	TYR B	138	5.381	9.273	−33.835	1	32.36	H
ATOM	2632	HD1	TYR B	138	2.939	9.593	−33.974	1	27.7	H
ATOM	2633	HD2	TYR B	138	4.705	6.626	−35.988	1	32.54	H
ATOM	2634	HE1	TYR B	138	0.883	8.612	−34.327	1	30.41	H
ATOM	2635	HE2	TYR B	138	2.65	5.641	−36.344	1	31.98	H
ATOM	2636	HH	TYR B	138	−0.257	6.909	−35.225	1	36.42	H
ATOM	2637	N	SER B	139	4.538	9.689	−37.87	1	26.36	N
ATOM	2638	CA	SER B	139	4.288	9.139	−39.207	1	27.55	C
ATOM	2639	C	SER B	139	3.526	10.099	−40.119	1	23.78	C
ATOM	2640	O	SER B	139	2.379	10.447	−39.841	1	22.07	O
ATOM	2641	CB	SER B	139	3.507	7.826	−39.099	1	25.84	C
ATOM	2642	OG	SER B	139	3.173	7.324	−40.386	1	25.64	O
ATOM	2643	H	SER B	139	3.936	10.241	−37.6	1	31.64	H
ATOM	2644	HA	SER B	139	5.14	8.944	−39.628	1	33.05	H
ATOM	2645	HB2	SER B	139	4.054	7.171	−38.638	1	31.01	H
ATOM	2646	HB3	SER B	139	2.69	7.985	−38.601	1	31.01	H
ATOM	2647	HG	SER B	139	3.872	7.181	−40.829	1	30.77	H
ATOM	2648	N	LYS B	140	4.161	10.507	−41.215	1	23.74	N
ATOM	2649	CA	LYS B	140	3.52	11.383	−42.19	1	25.13	C
ATOM	2650	C	LYS B	140	2.262	10.751	−42.772	1	27.27	C
ATOM	2651	O	LYS B	140	1.31	11.446	−43.124	1	23.6	O
ATOM	2652	CB	LYS B	140	4.479	11.725	−43.332	1	33.45	C
ATOM	2653	CG	LYS B	140	5.508	12.792	−43.013	1	30.77	C
ATOM	2654	CD	LYS B	140	6.309	13.145	−44.257	1	35.69	C
ATOM	2655	CE	LYS B	140	7.517	13.999	−43.925	1	38.62	C
ATOM	2656	NZ	LYS B	140	7.166	15.412	−43.646	1	40.07	N1+
ATOM	2657	H	LYS B	140	4.968	10.29	−41.417	1	28.48	H
ATOM	2658	HA	LYS B	140	3.265	12.211	−41.753	1	30.15	H
ATOM	2659	HB2	LYS B	140	4.961	10.921	−43.581	1	40.14	H
ATOM	2660	HB3	LYS B	140	3.959	12.039	−44.088	1	40.14	H
ATOM	2661	HG2	LYS B	140	5.058	13.592	−42.699	1	36.92	H
ATOM	2662	HG3	LYS B	140	6.119	12.46	−42.337	1	36.92	H
ATOM	2663	HD2	LYS B	140	6.621	12.329	−44.678	1	42.82	H
ATOM	2664	HD3	LYS B	140	5.745	13.643	−44.869	1	42.82	H
ATOM	2665	HE2	LYS B	140	7.953	13.637	−43.138	1	46.34	H
ATOM	2666	HE3	LYS B	140	8.129	13.985	−44.678	1	46.34	H
ATOM	2667	HZ1	LYS B	140	7.902	15.876	−43.456	1	48.08	H
ATOM	2668	HZ2	LYS B	140	6.771	15.773	−44.357	1	48.08	H
ATOM	2669	HZ3	LYS B	140	6.61	15.455	−42.952	1	48.08	H
ATOM	2670	N	GLU B	141	2.267	9.427	−42.874	1	25	N
ATOM	2671	CA	GLU B	141	1.193	8.708	−43.544	1	27.84	C
ATOM	2672	C	GLU B	141	0.014	8.489	−42.607	1	25.06	C
ATOM	2673	O	GLU B	141	−1.123	8.813	−42.942	1	27.37	O
ATOM	2674	CB	GLU B	141	1.7	7.367	−44.078	1	34.11	C
ATOM	2675	CG	GLU B	141	2.769	7.49	−45.16	1	36.43	C
ATOM	2676	CD	GLU B	141	4.098	8.026	−44.638	1	46.4	C
ATOM	2677	OE1	GLU B	141	4.499	7.656	−43.512	1	42.36	O
ATOM	2678	OE2	GLU B	141	4.74	8.824	−45.356	1	49.27	O1−
ATOM	2679	H	GLU B	141	2.886	8.919	−42.561	1	30	H
ATOM	2680	HA	GLU B	141	0.883	9.233	−44.298	1	33.41	H
ATOM	2681	HB2	GLU B	141	2.082	6.864	−43.342	1	40.93	H
ATOM	2682	HB3	GLU B	141	0.952	6.879	−44.455	1	40.93	H
ATOM	2683	HG2	GLU B	141	2.932	6.613	−45.543	1	43.71	H
ATOM	2684	HG3	GLU B	141	2.452	8.097	−45.847	1	43.71	H
ATOM	2685	N	ASP B	142	0.29	7.943	−41.429	1	28.26	N
ATOM	2686	CA	ASP B	142	−0.758	7.684	−40.452	1	24.57	C
ATOM	2687	C	ASP B	142	−1.332	8.975	−39.892	1	20.54	C
ATOM	2688	O	ASP B	142	−2.446	8.987	−39.375	1	22.29	O
ATOM	2689	CB	ASP B	142	−0.226	6.82	−39.31	1	25.59	C
ATOM	2690	CG	ASP B	142	0.03	5.39	−39.737	1	31.43	C
ATOM	2691	OD1	ASP B	142	−0.408	5.011	−40.844	1	33.75	O
ATOM	2692	OD2	ASP B	142	0.658	4.641	−38.96	1	36.61	O1−
ATOM	2693	H	ASP B	142	1.077	7.713	−41.171	1	33.91	H
ATOM	2694	HA	ASP B	142	−1.479	7.199	−40.884	1	29.48	H
ATOM	2695	HB2	ASP B	142	0.612	7.194	−38.994	1	30.71	H
ATOM	2696	HB3	ASP B	142	−0.877	6.807	−38.592	1	30.71	H
ATOM	2697	N	GLN B	143	−0.567	10.057	−39.996	1	21.57	N
ATOM	2698	CA	GLN B	143	−1.007	11.352	−39.489	1	22.32	C
ATOM	2699	C	GLN B	143	−1.076	12.372	−40.617	1	21.14	C
ATOM	2700	O	GLN B	143	−0.821	13.555	−40.412	1	19.64	O
ATOM	2701	CB	GLN B	143	−0.069	11.831	−38.383	1	16.49	C
ATOM	2702	CG	GLN B	143	0.132	10.792	−37.295	1	21.19	C
ATOM	2703	CD	GLN B	143	1.05	11.269	−36.196	1	21.57	C
ATOM	2704	OE1	GLN B	143	2.263	11.355	−36.384	1	19.08	O
ATOM	2705	NE2	GLN B	143	0.478	11.581	−35.039	1	19.58	N
ATOM	2706	H	GLN B	143	0.213	10.068	−40.356	1	25.88	H
ATOM	2707	HA	GLN B	143	−1.896	11.26	−39.112	1	26.78	H
ATOM	2708	HB2	GLN B	143	0.798	12.032	−38.769	1	19.78	H
ATOM	2709	HB3	GLN B	143	−0.443	12.626	−37.974	1	19.78	H
ATOM	2710	HG2	GLN B	143	−0.727	10.581	−36.897	1	25.43	H
ATOM	2711	HG3	GLN B	143	0.521	9.995	−37.686	1	25.43	H
ATOM	2712	HE21	GLN B	143	0.96	11.858	−34.382	1	23.5	H
ATOM	2713	HE22	GLN B	143	−0.374	11.507	−34.946	1	23.5	H
ATOM	2714	N	ASP B	144	−1.441	11.906	−41.808	1	23.98	N
ATOM	2715	CA	ASP B	144	−1.449	12.764	−42.986	1	24.23	C
ATOM	2716	C	ASP B	144	−2.493	13.879	−42.881	1	22.36	C
ATOM	2717	O	ASP B	144	−2.389	14.881	−43.582	1	21.23	O
ATOM	2718	CB	ASP B	144	−1.678	11.933	−44.256	1	28.7	C
ATOM	2719	CG	ASP B	144	−2.948	11.106	−44.203	1	27.6	C
ATOM	2720	OD1	ASP B	144	−3.543	10.979	−43.113	1	24.37	O
ATOM	2721	OD2	ASP B	144	−3.344	10.567	−45.258	1	40.47	O1−
ATOM	2722	H	ASP B	144	−1.689	11.096	−41.96	1	28.78	H
ATOM	2723	HA	ASP B	144	−0.579	13.185	−43.065	1	29.08	H
ATOM	2724	HB2	ASP B	144	−1.742	12.532	−45.016	1	34.44	H
ATOM	2725	HB3	ASP B	144	−0.93	11.326	−44.374	1	34.44	H
ATOM	2726	N	LEU B	145	−3.477	13.728	−41.996	1	19.04	N
ATOM	2727	CA	LEU B	145	−4.471	14.785	−41.804	1	22.41	C
ATOM	2728	C	LEU B	145	−3.812	16.062	−41.284	1	23.21	C
ATOM	2729	O	LEU B	145	−4.353	17.157	−41.44	1	16.02	O
ATOM	2730	CB	LEU B	145	−5.59	14.338	−40.849	1	23.82	C
ATOM	2731	CG	LEU B	145	−5.318	14.061	−39.362	1	27.11	C
ATOM	2732	CD1	LEU B	145	−5.111	15.321	−38.53	1	36.24	C
ATOM	2733	CD2	LEU B	145	−6.485	13.274	−38.783	1	26.9	C
ATOM	2734	H	LEU B	145	−3.591	13.034	−41.501	1	22.85	H
ATOM	2735	HA	LEU B	145	−4.878	14.99	−42.661	1	26.9	H
ATOM	2736	HB2	LEU B	145	−6.276	15.024	−40.873	1	28.59	H
ATOM	2737	HB3	LEU B	145	−5.962	13.519	−41.211	1	28.59	H
ATOM	2738	HG	LEU B	145	−4.52	13.515	−39.283	1	32.54	H
ATOM	2739	HD11	LEU B	145	−4.946	15.068	−37.609	1	43.49	H
ATOM	2740	HD12	LEU B	145	−4.349	15.809	−38.881	1	43.49	H
ATOM	2741	HD13	LEU B	145	−5.909	15.87	−38.585	1	43.49	H
ATOM	2742	HD21	LEU B	145	−6.571	12.437	−39.266	1	32.28	H
ATOM	2743	HD22	LEU B	145	−6.313	13.1	−37.845	1	32.28	H
ATOM	2744	HD23	LEU B	145	−7.296	13.797	−38.88	1	32.28	H
ATOM	2745	N	LEU B	146	−2.641	15.917	−40.669	1	18.69	N
ATOM	2746	CA	LEU B	146	−1.906	17.067	−40.147	1	20.59	C
ATOM	2747	C	LEU B	146	−1.461	18.011	−41.261	1	22.13	C
ATOM	2748	O	LEU B	146	−1.05	19.139	−40.994	1	20.52	O
ATOM	2749	CB	LEU B	146	−0.687	16.603	−39.346	1	17.78	C
ATOM	2750	CG	LEU B	146	−0.968	15.902	−38.018	1	17.5	C
ATOM	2751	CD1	LEU B	146	0.325	15.414	−37.395	1	17.27	C
ATOM	2752	CD2	LEU B	146	−1.696	16.837	−37.055	1	20.64	C
ATOM	2753	H	LEU B	146	−2.25	15.162	−40.542	1	22.42	H
ATOM	2754	HA	LEU B	146	−2.485	17.564	−39.548	1	24.71	H
ATOM	2755	HB2	LEU B	146	−0.181	15.984	−39.896	1	21.34	H
ATOM	2756	HB3	LEU B	146	−0.14	17.38	−39.151	1	21.34	H
ATOM	2757	HG	LEU B	146	−1.536	15.132	−38.178	1	21	H
ATOM	2758	HD11	LEU B	146	0.123	14.973	−36.555	1	20.72	H
ATOM	2759	HD12	LEU B	146	0.751	14.789	−38.003	1	20.72	H
ATOM	2760	HD13	LEU B	146	0.907	16.174	−37.239	1	20.72	H
ATOM	2761	HD21	LEU B	146	−1.861	16.367	−36.223	1	24.77	H
ATOM	2762	HD22	LEU B	146	−1.142	17.615	−36.892	1	24.77	H
ATOM	2763	HD23	LEU B	146	−2.538	17.108	−37.455	1	24.77	H
ATOM	2764	N	LYS B	147	−1.546	17.549	−42.505	1	18.08	N
ATOM	2765	CA	LYS B	147	−1.162	18.363	−43.656	1	21.55	C
ATOM	2766	C	LYS B	147	−2.1	19.543	−43.918	1	18.51	C
ATOM	2767	O	LYS B	147	−1.684	20.547	−44.493	1	21.96	O
ATOM	2768	CB	LYS B	147	−1.098	17.501	−44.915	1	21.16	C
ATOM	2769	CG	LYS B	147	0.074	16.547	−44.957	1	30.69	C
ATOM	2770	CD	LYS B	147	0.195	15.878	−46.321	1	36.31	C
ATOM	2771	CE	LYS B	147	−0.442	14.498	−46.326	1	47.69	C
ATOM	2772	NZ	LYS B	147	−0.373	13.845	−47.665	1	54.63	N1+
ATOM	2773	H	LYS B	147	−1.824	16.762	−42.711	1	21.7	H
ATOM	2774	HA	LYS B	147	−0.275	18.723	−43.499	1	25.85	H
ATOM	2775	HB2	LYS B	147	−1.91	16.973	−44.972	1	25.39	H
ATOM	2776	HB3	LYS B	147	−1.032	18.084	−45.688	1	25.39	H
ATOM	2777	HG2	LYS B	147	0.893	17.037	−44.784	1	36.83	H
ATOM	2778	HG3	LYS B	147	−0.052	15.855	−44.289	1	36.83	H
ATOM	2779	HD2	LYS B	147	−0.255	16.423	−46.986	1	43.57	H
ATOM	2780	HD3	LYS B	147	1.134	15.78	−46.547	1	43.57	H
ATOM	2781	HE2	LYS B	147	0.023	13.931	−45.691	1	57.23	H
ATOM	2782	HE3	LYS B	147	−1.376	14.579	−46.078	1	57.23	H
ATOM	2783	HZ1	LYS B	147	0.476	13.753	−47.915	1	65.55	H
ATOM	2784	HZ2	LYS B	147	−0.754	13.042	−47.632	1	65.55	H
ATOM	2785	HZ3	LYS B	147	−0.799	14.343	−48.268	1	65.55	H
ATOM	2786	N	LEU B		148	−3.362	19.42	−43.518	1	18.78	N
ATOM	2787	CA	LEU B	148	−4.353	20.45	−43.829	1	22.97	C
ATOM	2788	C	LEU B	148	−4.868	21.167	−42.585	1	14.82	C
ATOM	2789	O	LEU B	148	−6.011	21.617	−42.541	1	14.64	O
ATOM	2790	CB	LEU B	148	−5.517	19.832	−44.607	1	26	C
ATOM	2791	CG	LEU B		148	−5.16	19.38	−46.029	1	31.59	C
ATOM	2792	CD1	LEU B	148	−6.356	18.716	−46.679	1	33.85	C
ATOM	2793	CD2	LEU B		148	−4.67	20.547	−46.891	1	31.17	C
ATOM	2794	H	LEU B		148	−3.67	18.755	−43.068	1	22.53	H
ATOM	2795	HA	LEU B		148	−3.939	21.115	−44.401	1	27.56	H
ATOM	2796	HB2	LEU B	148	−5.837	19.055	−44.123	1	31.2	H
ATOM	2797	HB3	LEU B	148	−6.228	20.489	−44.677	1	31.2	H
ATOM	2798	HG	LEU B	148	−4.446	18.725	−45.98	1	37.91	H
ATOM	2799	HD11	LEU B	148	−6.113	18.437	−47.575	1	40.61	H
ATOM	2800	HD12	LEU B	148	−6.614	17.944	−46.15	1	40.61	H
ATOM	2801	HD13	LEU B	148	−7.088	19.351	−46.716	1	40.61	H
ATOM	2802	HD21	LEU B	148	−3.878	20.931	−46.481	1	37.4	H
ATOM	2803	HD22	LEU B	148	−4.456	20.216	−47.778	1	37.4	H
ATOM	2804	HD23	LEU B	148	−5.371	21.215	−46.946	1	37.4	H
ATOM	2805	N	VAL B	149	−4	21.295	−41.587	1	21.37	N
ATOM	2806	CA	VAL B	149	−4.324	22.025	−40.365	1	16	C
ATOM	2807	C	VAL B	149	−3.814	23.459	−40.465	1	15.16	C
ATOM	2808	O	VAL B		149	−2.619	23.685	−40.651	1	17.77	O
ATOM	2809	CB	VAL B	149	−3.708	21.343	−39.13	1	15.06	C
ATOM	2810	CG1	VAL B	149	−4.064	22.1	−37.853	1	19.91	C
ATOM	2811	CG2	VAL B	149	−4.179	19.899	−39.037	1	22.08	C
ATOM	2812	H	VAL B		149	−3.206	20.964	−41.594	1	25.65	H
ATOM	2813	HA	VAL B		149	−5.287	22.05	−40.252	1	19.19	H
ATOM	2814	HB	VAL B	149	−2.742	21.34	−39.219	1	18.07	H
ATOM	2815	HG11	VAL B	149	−3.662	21.646	−37.096	1	23.89	H
ATOM	2816	HG12	VAL B	149	−3.721	23.005	−37.917	1	23.89	H
ATOM	2817	HG13	VAL B	149	−5.028	22.118	−37.755	1	23.89	H
ATOM	2818	HG21	VAL B	149	−3.781	19.488	−38.254	1	26.49	H
ATOM	2819	HG22	VAL B	149	−5.146	19.886	−38.963	1	26.49	H
ATOM	2820	HG23	VAL B	149	−3.902	19.425	−39.837	1	26.49	H
ATOM	2821	N	LYS B	150	−4.723	24.422	−40.354	1	13.81	N
ATOM	2822	CA	LYS B	150	−4.346	25.833	−40.34	1	15.89	C
ATOM	2823	C	LYS B	150	−3.784	26.238	−38.987	1	14.81	C
ATOM	2824	O	LYS B	150	−3.953	25.531	−37.996	1	17.84	O
ATOM	2825	CB	LYS B	150	−5.542	26.729	−40.663	1	19.83	C
ATOM	2826	CG	LYS B	150	−5.939	26.78	−42.121	1	18.05	C
ATOM	2827	CD	LYS B	150	−6.947	27.893	−42.372	1	16	C
ATOM	2828	CE	LYS B	150	−6.287	29.264	−42.452	1	20.31	C
ATOM	2829	NZ	LYS B	150	−5.422	29.408	−43.661	1	20.83	N1+
ATOM	2830	H	LYS B	150	−5.569	24.285	−40.285	1	16.58	H
ATOM	2831	HA	LYS B	150	−3.663	25.986	−41.011	1	19.07	H
ATOM	2832	HB2	LYS B	150	−6.31	26.409	−40.163	1	23.79	H
ATOM	2833	HB3	LYS B	150	−5.331	27.634	−40.386	1	23.79	H
ATOM	2834	HG2	LYS B	150	−5.153	26.952	−42.662	1	21.66	H
ATOM	2835	HG3	LYS B	150	−6.346	25.937	−42.373	1	21.66	H
ATOM	2836	HD2	LYS B	150	−7.4	27.728	−43.214	1	19.21	H
ATOM	2837	HD3	LYS B	150	−7.589	27.91	−41.645	1	19.21	H
ATOM	2838	HE2	LYS B	150	−6.976	29.946	−42.491	1	24.37	H
ATOM	2839	HE3	LYS B	150	−5.732	29.395	−41.667	1	24.37	H
ATOM	2840	HZ1	LYS B	150	−5.053	30.217	−43.676	1	25	H
ATOM	2841	HZ2	LYS B	150	−4.776	28.796	−43.647	1	25	H
ATOM	2842	HZ3	LYS B		150	−5.908	29.297	−44.398	1	25	H
ATOM	2843	N	SER B	151	−3.129	27.394	−38.963	1	16.36	N
ATOM	2844	CA	SER B	151	−2.654	28.008	−37.729	1	15.93	C
ATOM	2845	C	SER B	151	−1.536	27.201	−37.075	1	14.66	C
ATOM	2846	O	SER B	151	−1.004	26.253	−37.656	1	15.81	O
ATOM	2847	CB	SER B	151	−3.817	28.195	−36.746	1	16.71	C
ATOM	2848	OG	SER B	151	−3.442	29.042	−35.672	1	18.88	O
ATOM	2849	H	SER B	151	−2.944	27.853	−39.666	1	19.63	H
ATOM	2850	HA	SER B	151	−2.3	28.887	−37.937	1	19.12	H
ATOM	2851	HB2	SER B	151	−4.566	28.593	−37.215	1	20.05	H
ATOM	2852	HB3	SER B	151	−4.071	27.329	−36.39	1	20.05	H
ATOM	2853	HG	SER B	151	−4.087	29.136	−35.142	1	22.66	H
ATOM	2854	N	TYR B	152	−1.184	27.604	−35.862	1	13.42	N
ATOM	2855	CA	TYR B	152	−0.041	27.051	−35.15	1	12.43	C
ATOM	2856	C	TYR B	152	−0.498	26.485	−33.816	1	12.59	C
ATOM	2857	O	TYR B	152	−1.349	27.075	−33.152	1	14.9	O
ATOM	2858	CB	TYR B	152	1.015	28.128	−34.925	1	11.01	C
ATOM	2859	CG	TYR B	152	1.401	28.904	−36.165	1	14.74	C
ATOM	2860	CD1	TYR B	152	1.697	28.254	−37.356	1	14.53	C
ATOM	2861	CD2	TYR B	152	1.476	30.291	−36.14	1	16.11	C
ATOM	2862	CE1	TYR B	152	2.063	28.964	−38.488	1	19.24	C
ATOM	2863	CE2	TYR B	152	1.837	31.011	−37.265	1	13.65	C
ATOM	2864	CZ	TYR B	152	2.132	30.343	−38.436	1	18.79	C
ATOM	2865	OH	TYR B	152	2.492	31.058	−39.558	1	16.6	O
ATOM	2866	H	TYR B	152	−1.602	28.212	−35.42	1	16.1	H
ATOM	2867	HA	TYR B	152	0.353	26.334	−35.672	1	14.92	H
ATOM	2868	HB2	TYR B	152	0.676	28.764	−34.276	1	13.21	H
ATOM	2869	HB3	TYR B	152	1.818	27.708	−34.581	1	13.21	H
ATOM	2870	HD1	TYR B	152	1.656	27.325	−37.393	1	17.43	H
ATOM	2871	HD2	TYR B	152	1.283	30.744	−35.351	1	19.33	H
ATOM	2872	HE1	TYR B	152	2.259	28.516	−39.278	1	23.09	H
ATOM	2873	HE2	TYR B	152	1.884	31.939	−37.231	1	16.38	H
ATOM	2874	HH	TYR B	152	2.493	31.88	−39.386	1	19.92	H
ATOM	2875	N	HIS B	153	0.066	25.347	−33.423	1	12.19	N
ATOM	2876	CA	HIS B	153	−0.389	24.651	−32.228	1	14.36	C
ATOM	2877	C	HIS B	153	0.758	23.957	−31.495	1	13.41	C
ATOM	2878	O	HIS B	153	1.626	23.342	−32.118	1	12.89	O
ATOM	2879	CB	HIS B	153	1.464	23.627	−32.601	1	15.15	C
ATOM	2880	CG	HIS B	153	−2.473	24.146	−33.578	1	14.4	C
ATOM	2881	ND1	HIS B	153	−3.664	24.719	−33.187	1	12.28	N
ATOM	2882	CD2	HIS B	153	−2.459	24.195	−34.932	1	15.15	C
ATOM	2883	CE1	HIS B	153	−4.344	25.088	−34.257	1	14.83	C
ATOM	2884	NE2	HIS B	153	−3.635	24.783	−35.329	1	14.05	N
ATOM	2885	H	HIS B	153	0.714	24.958	−33.833	1	14.63	H
ATOM	2886	HA	HIS B	153	−0.787	25.294	−31.621	1	17.23	H
ATOM	2887	HB2	HIS B	153	−1.035	22.854	−32.999	1	18.18	H
ATOM	2888	HB3	HIS B	153	−1.937	23.364	−31.796	1	18.18	H
ATOM	2889	HD1	HIS B	153	−3.926	24.816	−32.373	1	14.73	H
ATOM	2890	HD2	HIS B	153	−1.781	23.885	−35.488	1	18.18	H
ATOM	2891	HE1	HIS B	153	−5.18	25.496	−34.257	1	17.79	H
ATOM	2892	HE2	HIS B	153	−3.871	24.928	−36.143	1	16.86	H
ATOM	2893	N	TRP B	154	0.757	24.065	−30.169	1	14.83	N
ATOM	2894	CA	TRP B	154	1.722	23.341	−29.353	1	15.59	C
ATOM	2895	C	TRP B	154	1.638	21.838	−29.612	1	15.56	C
ATOM	2896	O	TRP B	154	0.546	21.257	−29.644	1	12.57	O
ATOM	2897	CB	TRP B	154	1.497	23.599	−27.86	1	17.58	C
ATOM	2898	CG	TRP B	154	1.962	24.933	−27.34	1	16.06	C
ATOM	2899	CD1	TRP B	154	1.23	25.821	−26.606	1	18.33	C
ATOM	2900	CD2	TRP B	154	3.265	25.515	−27.489	1	12.92	C
ATOM	2901	NE1	TRP B	154	1.993	26.922	−26.293	1	15.98	N
ATOM	2902	CE2	TRP B	154	3.244	26.76	−26.825	1	16.75	C
ATOM	2903	CE3	TRP B	154	4.441	25.112	−28.125	1	14.07	C
ATOM	2904	CZ2	TRP B	154	4.357	27.6	−26.777	1	16.96	C
ATOM	2905	CZ3	TRP B	154	5.543	25.946	−28.075	1	13.07	C
ATOM	2906	CH2	TRP B	154	5.493	27.176	−27.407	1	16.27	C
ATOM	2907	H	TRP B	154	0.208	24.551	−29.72	1	17.8	H
ATOM	2908	HA	TRP B	154	2.617	23.638	−29.58	1	18.71	H
ATOM	2909	HB2	TRP B	154	0.546	23.535	−27.681	1	21.1	H
ATOM	2910	HB3	TRP B	154	1.966	22.914	−27.359	1	21.1	H
ATOM	2911	HD1	TRP B	154	0.345	25.698	−26.35	1	22	H
ATOM	2912	HE1	TRP B	154	1.726	27.602	−25.839	1	19.17	H
ATOM	2913	HE3	TRP B	154	4.484	24.295	−28.568	1	16.88	H
ATOM	2914	HZ2	TRP B	154	4.325	28.418	−26.337	1	20.35	H
ATOM	2915	HZ3	TRP B	154	6.332	25.686	−28.493	1	15.69	H
ATOM	2916	HH2	TRP B	154	6.249	27.717	−27.393	1	19.52	H
ATOM	2917	N	MET B	155	2.802	21.229	−29.81	1	9.94	N
ATOM	2918	CA	MET B	155	2.946	19.779	−29.802	1	14.74	C
ATOM	2919	C	MET B	155	3.944	19.396	−28.711	1	16.06	C
ATOM	2920	O	MET B	155	4.555	20.265	−28.092	1	15.26	O
ATOM	2921	CB	MET B	155	3.401	19.261	−31.167	1	14.63	C
ATOM	2922	CG	MET B	155	4.639	19.948	−31.731	1	14.92	C
ATOM	2923	SD	MET B	155	5.043	19.295	−33.366	1	14.73	S
ATOM	2924	CE	MET B	155	6.245	20.481	−33.946	1	14.31	C
ATOM	2925	H	MET B	155	3.541	21.645	−29.955	1	11.93	H
ATOM	2926	HA	MET B	155	2.086	19.377	−29.6	1	17.69	H
ATOM	2927	HB2	MET B	155	3.601	18.315	−31.088	1	17.56	H
ATOM	2928	HB3	MET B	155	2.68	19.389	−31.803	1	17.56	H
ATOM	2929	HG2	MET B	155	4.47	20.9	−31.814	1	17.9	H
ATOM	2930	HG3	MET B	155	5.393	19.789	−31.142	1	17.9	H
ATOM	2931	HE1	MET B	155	6.539	20.224	−34.834	1	17.17	H
ATOM	2932	HE2	MET B	155	5.834	21.359	−33.973	1	17.17	H
ATOM	2933	HE3	MET B	155	7	20.487	−33.337	1	17.17	H
ATOM	2934	N	GLY B	156	4.118	18.098	−28.488	1	16.14	N
ATOM	2935	CA	GLY B	156	4.866	17.615	−27.341	1	17.15	C
ATOM	2936	C	GLY B	156	6.372	17.566	−27.518	1	20.32	C
ATOM	2937	O	GLY B	156	7.04	16.765	−26.871	1	22.44	O
ATOM	2938	H	GLY B	156	3.809	17.474	−28.993	1	19.37	H
ATOM	2939	HA2	GLY B	156	4.674	18.186	−26.58	1	20.58	H
ATOM	2940	HA3	GLY B	156	4.563	16.719	−27.125	1	20.58	H
ATOM	2941	N	LEU B	157	6.907	18.425	−28.379	1	19.69	N
ATOM	2942	CA	LEU B	157	8.338	18.436	−28.667	1	18.9	C
ATOM	2943	C	LEU B	157	9.056	19.485	−27.826	1	26.5	C
ATOM	2944	O	LEU B	157	8.641	20.647	−27.784	1	20.35	O
ATOM	2945	CB	LEU B	157	8.575	18.704	−30.151	1	21.54	C
ATOM	2946	CG	LEU B	157	9.956	18.345	−30.698	1	24.32	C
ATOM	2947	CD1	LEU B	157	10.18	16.839	−30.673	1	23	C
ATOM	2948	CD2	LEU B	157	10.107	18.882	−32.106	1	21.66	C
ATOM	2949	H	LEU B	157	6.459	19.017	−28.813	1	23.63	H
ATOM	2950	HA	LEU B	157	8.713	17.567	−28.453	1	22.67	H
ATOM	2951	HB2	LEU B	157	7.924	18.195	−30.659	1	25.85	H
ATOM	2952	HB3	LEU B	157	B.44	19.651	−30.313	1	25.85	H
ATOM	2953	HG	LEU B	157	10.635	18.76	−30.143	1	29.18	H
ATOM	2954	HD11	LEU B	157	11.063	16.646	−31.026	1	27.6	H
ATOM	2955	HD12	LEU B	157	10.114	16.526	−29.757	1	27.6	H
ATOM	2956	HD13	LEU B	157	9.504	16.411	−31.22	1	27.6	H
ATOM	2957	HD21	LEU B	157	10.986	18.647	−32.441	1	25.99	H
ATOM	2958	HD22	LEU B	157	9.422	18.488	−32.669	1	25.99	H
ATOM	2959	HD23	LEU B	157	10.006	19.847	−32.088	1	25.99	H
ATOM	2960	N	VAL B	158	10.131	19.072	−27.16	1	22.65	N
ATOM	2961	CA	VAL B	158	10.884	19.968	−26.289	1	21.67	C
ATOM	2962	C	VAL B	158	12.384	19.821	−26.504	1	23.85	C
ATOM	2963	O	VAL B	158	12.879	18.732	−26.798	1	21.21	O
ATOM	2964	CB	VAL B	158	10.56	19.711	−24.804	1	27.43	C
ATOM	2965	CG1	VAL B	158	9.115	20.099	−24.502	1	26.57	C
ATOM	2966	CG2	VAL B	158	10.814	18.253	−24.446	1	29.47	C
ATOM	2967	H	VAL B	158	10.447	18.273	−27.197	1	27.18	H
ATOM	2968	HA	VAL B	158	10.641	20.885	−26.494	1	26.01	H
ATOM	2969	HB	VAL B	158	11.139	20.261	−24.254	1	32.92	H
ATOM	2970	HG11	VAL B	158	8.933	19.929	−23.565	1	31.88	H
ATOM	2971	HG12	VAL B	158	8.995	21.041	−24.698	1	31.88	H
ATOM	2972	HG13	VAL B	158	8.524	19.567	−25.056	1	31.88	H
ATOM	2973	HG21	VAL B	158	10.602	18.117	−23.509	1	35.36	H
ATOM	2974	HG22	VAL B	158	10.249	17.689	−24.998	1	35.36	H
ATOM	2975	HG23	VAL B	158	11.747	18.046	−24.608	1	35.36	H
ATOM	2976	N	HIS B	159	13.096	20.933	−26.357	1	22.33	N
ATOM	2977	CA	HIS B	159	14.541	20.959	−26.523	1	29.47	C
ATOM	2978	C	HIS B	159	15.215	20.956	−25.158	1	41.69	C
ATOM	2979	0	HIS B	159	14.926	21.802	−24.315	1	37.55	O
ATOM	2980	CB	HIS B	159	14.961	22.189	−27.327	1	33.99	C
ATOM	2981	CG	HIS B	159	16.43	22.259	−27.601	1	41.87	C
ATOM	2982	ND1	HIS B	159	17.272	23.12	−26.929	1	45.71	N
ATOM	2983	CD2	HIS B	159	17.207	21.576	−28.474	1	42.1	C
ATOM	2984	CE1	HIS B	159	18.505	22.962	−27.377	1	52.16	C
ATOM	2985	NE2	HIS B	159	18.492	22.032	−28.314	1	50.26	N
ATOM	2986	H	HIS B	159	12.757	21.698	−26.158	1	26.8	H
ATOM	2987	HA	HIS B	159	14.824	20.167	−27.006	1	35.36	H
ATOM	2988	HB2	HIS B	159	14.501	22.177	−28.18	1	40.79	H
ATOM	2989	HB3	HIS B	159	14.714	22.985	−26.831	1	40.79	H
ATOM	2990	HD1	HIS B	159	17.033	23.672	−26.315	1	54.85	H
ATOM	2991	HD2	HIS B	159	16.923	20.92	−29.07	1	50.52	H
ATOM	2992	HE1	HIS B	159	19.255	23.428	−27.083	1	62.6	H
ATOM	2993	HE2	HIS B	159	19.178	21.757	−28.754	1	60.31	H
ATOM	2994	N	ILE B	160	16.102	19.991	−24.944	1	47.95	N
ATOM	2995	CA	ILE B	160	16.84	19.885	−23.692	1	58.27	C
ATOM	2996	C	ILE B	160	18.248	20.455	−23.88	1	66.09	C
ATOM	2997	O	ILE B	160	19.148	19.743	−24.324	1	70.94	O
ATOM	2998	CB	ILE B	160	16.936	18.419	−23.208	1	63.95	C
ATOM	2999	CG1	ILE B	160	15.588	17.704	−23.348	1	56.29	C
ATOM	3000	CG2	ILE B	160	17.414	18.368	−21.768	1	67.71	C
ATOM	3001	CD1	ILE B	160	14.461	18.326	−22.545	1	48.29	C
ATOM	3002	H	ILE B	160	16.295	19.377	−25.514	1	57.54	H
ATOM	3003	HA	ILE B	160	16.389	20.404	−23.007	1	69.92	H
ATOM	3004	HB	ILE B	160	17.585	17.958	−23.761	1	76.73	H
ATOM	3005	HG12	ILE B	160	15.326	17.717	−24.282	1	67.54	H
ATOM	3006	HG13	ILE B	160	15.69	16.787	−23.05	1	67.54	H
ATOM	3007	HG21	ILE B	160	17.467	17.442	−21.486	1	81.25	H
ATOM	3008	HG22	ILE B	160	18.29	18.782	−21.712	1	81.25	H
ATOM	3009	HG23	ILE B	160	16.784	18.849	−21.209	1	81.25	H
ATOM	3010	HD11	ILE B	160	13.65	17.815	−22.691	1	57.95	H
ATOM	3011	HD12	ILE B	160	14.698	18.311	−21.605	1	57.95	H
ATOM	3012	HD13	ILE B	160	14.332	19.242	−22.839	1	57.95	H
ATOM	3013	N	PRO B	161	18.448	21.748	−23.558	1	69.7	N
ATOM	3014	CA	PRO B	161	19.784	22.316	−23.778	1	73.07	C
ATOM	3015	C	PRO B	161	20.833	21.764	−22.813	1	80.56	C
ATOM	3016	O	PRO B	161	20.862	22.147	−21.644	1	84.37	O
ATOM	3017	CB	PRO B	161	19.57	23.817	−23.556	1	69.03	C
ATOM	3018	CG	PRO B	161	18.392	23.902	−22.659	1	63.55	C
ATOM	3019	CD	PRO B	161	17.503	22.758	−23.048	1	60.94	C
ATOM	3020	HA	PRO B	161	20.072	22.162	−24.692	1	87.68	H
ATOM	3021	HB2	PRO B	161	20.354	24.2	−23.132	1	82.83	H
ATOM	3022	HB3	PRO B	161	19.39	24.251	−24.404	1	82.83	H
ATOM	3023	HG2	PRO B	161	18.678	23.814	−21.737	1	76.25	H
ATOM	3024	HG3	PRO B	161	17.939	24.749	−22.798	1	76.25	H
ATOM	3025	HD2	PRO B	161	17.031	22.417	−22.272	1	73.12	H
ATOM	3026	HD3	PRO B	161	16.888	23.029	−23.748	1	73.12	H
ATOM	3027	N	THR B	162	21.679	20.88	−23.334	1	82.8	N
ATOM	3028	CA	THR B	162	22.732	20.185	−22.591	1	89.98	C
ATOM	3029	C	THR B	162	23.165	19.019	−23.47	1	91.72	C
ATOM	3030	O	THR B	162	24.34	18.653	−23.513	1	95.85	O
ATOM	3031	CB	THR B	162	22.284	19.66	−21.201	1	95.35	C
ATOM	3032	OG1	THR B	162	23.364	18.945	−20.585	1	96.68	O
ATOM	3033	CG2	THR B	162	21.08	18.741	−21.324	1	98.91	C
ATOM	3034	H	THR B	162	21.661	20.654	−24.164	1	99.36	H
ATOM	3035	HA	THR B	162	23.49	20.778	−22.468	1	107.98	H
ATOM	3036	HB	THR B	162	22.037	20.412	−20.64	1	114.42	H
ATOM	3037	HG1	THR B	162	23.588	18.294	−21.066	1	116.01	H
ATOM	3038	HG21	THR B	162	20.815	18.424	−20.446	1	118.69	H
ATOM	3039	HG22	THR B	162	20.337	19.22	−21.724	1	118.69	H
ATOM	3040	HG23	THR B	162	21.301	17.979	−21.881	1	118.69	H
ATOM	3041	N	ASN B	163	22.186	18.447	−24.166	1	91.1	N
ATOM	3042	CA	ASN B	163	22.418	17.423	−25.177	1	91.71	C
ATOM	3043	C	ASN B	163	22.143	17.982	−26.573	1	82.79	C
ATOM	3044	O	ASN B	163	22.538	17.393	−27.58	1	78.88	O
ATOM	3045	CB	ASN B	163	21.543	16.19	−24.907	1	94.16	C
ATOM	3046	CG	ASN B	163	20.053	16.513	−24.865	1	93.87	C
ATOM	3047	OD1	ASN B	163	19.539	17.272	−25.687	1	91.61	O
ATOM	3048	ND2	ASN B	163	19.353	15.925	−23.9	1	94.1	N
ATOM	3049	H	ASN B	163	21.354	18.643	−24.066	1	109.32	H
ATOM	3050	HA	ASN B	163	23.347	17.147	−25.141	1	110.05	H
ATOM	3051	HB2	ASN B	163	21.688	15.54	−25.612	1	112.99	H
ATOM	3052	HB3	ASN B	163	21.791	15.81	−24.05	1	112.99	H
ATOM	3053	HD21	ASN B	163	18.509	16.073	−23.831	1	112.92	H
ATOM	3054	HD22	ASN B	163	19.744	15.398	−23.345	1	112.92	H
ATOM	3055	N	GLY B	164	21.463	19.124	−26.622	1	81.6	N
ATOM	3056	CA	GLY B	164	21.145	19.781	−27.877	1	76.23	C
ATOM	3057	C	GLY B	164	20.312	18.905	−28.793	1	73.18	C
ATOM	3058	O	GLY B	164	20.669	18.689	−29.951	1	76.11	O
ATOM	3059	H	GLY B	164	21.172	19.542	−25.929	1	97.92	H
ATOM	3060	HA2	GLY B	164	20.652	20.597	−27.7	1	91.48	H
ATOM	3061	HA3	GLY B	164	21.967	20.012	−28.338	1	91.48	H
ATOM	3062	N	SER B	165	19.2	18.399	−28.269	1	64.95	N
ATOM	3063	CA	SER B	165	18.326	17.518	−29.031	1	57.43	C
ATOM	3064	C	SER B	165	16.861	17.81	−28.744	1	45.57	C
ATOM	3065	O	SER B	165	16.511	18.287	−27.663	1	44.26	O
ATOM	3066	CB	SER B	165	18.635	16.056	−28.711	1	62.72	C
ATOM	3067	OG	SER B	165	18.321	15.754	−27.362	1	67.74	O
ATOM	3068	H	SER B	165	18.928	18.554	−27.468	1	77.94	H
ATOM	3069	HA	SER B	165	18.481	17.659	−29.978	1	68.91	H
ATOM	3070	HB2	SER B	165	18.106	15.488	−29.292	1	75.26	H
ATOM	3071	HB3	SER B	165	19.58	15.894	−28.859	1	75.26	H
ATOM	3072	HG	SER B	165	17.505	15.89	−27.219	1	81.29	H
ATOM	3073	N	TRP B	166	16.012	17.515	−29.723	1	40.98	N
ATOM	3074	CA	TRP B	166	14.569	17.656	−29.572	1	34.55	C
ATOM	3075	C	TRP B	166	13.945	16.298	−29.288	1	31.08	C
ATOM	3076	O	TRP B	166	14.212	15.33	−29.999	1	34.34	O
ATOM	3077	CB	TRP B	166	13.953	18.265	−30.83	1	30.13	C
ATOM	3078	CG	TRP B	166	14.302	19.703	−31.041	1	30.81	C
ATOM	3079	CD1	TRP B	166	15.354	20.196	−31.756	1	36.26	C
ATOM	3080	CD2	TRP B	166	13.591	20.841	−30.538	1	28.21	C
ATOM	3081	NE1	TRP B	166	15.344	21.569	−31.726	1	34.03	N
ATOM	3082	CE2	TRP B	166	14.272	21.99	−30.984	1	27.63	C
ATOM	3083	CE3	TRP B	166	12.446	20.999	−29.751	1	23.82	C
ATOM	3084	CZ2	TRP B	166	13.846	23.28	−30.671	1	27.91	C
ATOM	3085	CZ3	TRP B	166	12.024	22.281	−29.44	1	24.12	C
ATOM	3086	CH2	TRP B	166	12.722	23.405	−29.901	1	25.08	C
ATOM	3087	H	TRP B	166	16.252	17.226	−30.496	1	49.18	H
ATOM	3088	HA	TRP B	166	14.379	18.243	−28.824	1	41.46	H
ATOM	3089	HB2	TRP B	166	14.265	17.769	−31.603	1	36.16	H
ATOM	3090	HB3	TRP B	166	12.987	18.201	−30.767	1	36.16	H
ATOM	3091	HD1	TRP B	166	15.987	19.677	−32.198	1	43.51	H
ATOM	3092	HE1	TRP B	166	15.918	22.081	−32.111	1	40.83	H
ATOM	3093	HE3	TRP B	166	11.977	20.257	−29.442	1	28.59	H
ATOM	3094	HZ2	TRP B	166	14.308	24.028	−30.975	1	33.49	H
ATOM	3095	HZ3	TRP B	166	11.263	22.398	−28.918	1	28.94	H
ATOM	3096	HH2	TRP B	166	12.416	24.254	−29.676	1	30.1	H
ATOM	3097	N	GLN B	167	13.119	16.225	−28.25	1	27.39	N
ATOM	3098	CA	GLN B	167	12.485	14.965	−27.879	1	30.85	C
ATOM	3099	C	GLN B	167	11.02	15.147	−27.492	1	26.83	C
ATOM	3100	O	GLN B	167	10.604	16.219	−27.048	1	24.25	O
ATOM	3101	CB	GLN B	167	13.248	14.306	−26.729	1	31.47	C
ATOM	3102	CG	GLN B	167	13.319	15.142	−25.462	1	39.54	C
ATOM	3103	CD	GLN B	167	13.995	14.409	−24.315	1	47.76	C
ATOM	3104	OE1	GLN B	167	13.559	14.498	−23.168	1	47.44	O
ATOM	3105	NE2	GLN B	167	15.066	13.683	−24.618	1	48.92	N
ATOM	3106	H	GLN B	167	12.91	16.889	−27.745	1	32.87	H
ATOM	3107	HA	GLN B	167	12.517	14.364	−28.639	1	37.02	H
ATOM	3108	HB2	GLN B	167	12.811	13.469	−26.505	1	37.76	H
ATOM	3109	HB3	GLN B	167	14.157	14.132	−27.018	1	37.76	H
ATOM	3110	HG2	GLN B	167	13.827	15.949	−25.644	1	47.45	H
ATOM	3111	HG3	GLN B	167	12.419	15.371	−25.183	1	47.45	H
ATOM	3112	HE21	GLN B	167	15.482	13.251	−24.002	1	58.7	H
ATOM	3113	HE22	GLN B	167	15.344	13.645	−25.431	1	58.7	H
ATOM	3114	N	TRP B	168	10.249	14.079	−27.668	1	23.01	N
ATOM	3115	CA	TRP B	168	8.838	14.077	−27.318	1	26.18	C
ATOM	3116	C	TRP B	168	8.659	13.855	−25.826	1	24.45	C
ATOM	3117	O	TRP B	168	9.611	13.512	−25.128	1	28.38	O
ATOM	3118	CB	TRP B	168	8.1	13	−28.108	1	25.3	C
ATOM	3119	CG	TRP B	168	8.224	13.197	−29.577	1	26.32	C
ATOM	3120	CD1	TRP B	168	8.994	12.476	−30.439	1	25.09	C
ATOM	3121	CD2	TRP B	168	7.571	14.198	−30.361	1	22.02	C
ATOM	3122	NE1	TRP B	168	8.856	12.963	−31.716	1	23.33	N
ATOM	3123	CE2	TRP B	168	7.985	14.02	−31.694	1	23.22	C
ATOM	3124	CE3	TRP B	168	6.67	15.228	−30.064	1	25.48	C
ATOM	3125	CZ2	TRP B	168	7.532	14.832	−32.731	1	20.73	C
ATOM	3126	CZ3	TRP B	168	6.22	16.029	−31.093	1	20.54	C
ATOM	3127	CH2	TRP B	168	6.653	15.829	−32.41	1	19.21	C
ATOM	3128	H	TRP B	168	10.527	13.334	−27.995	1	27.61	H
ATOM	3129	HA	TRP B	168	8.452	14.937	−27.544	1	31.42	H
ATOM	3130	HB2	TRP B	168	8.473	12.133	−27.888	1	30.36	H
ATOM	3131	HB3	TRP B	168	7.158	13.027	−27.879	1	30.36	H
ATOM	3132	HD1	TRP B	168	9.534	11.758	−30.198	1	30.11	H
ATOM	3133	HE1	TRP B	168	9.25	12.653	−32.415	1	28	H
ATOM	3134	HE3	TRP B	168	6.379	15.367	−29.192	1	30.57	H
ATOM	3135	HZ2	TRP B	168	7.815	14.701	−33.607	1	24.88	H
ATOM	3136	HZ3	TRP B	168	5.622	16.717	−30.909	1	24.65	H
ATOM	3137	HH2	TRP B	168	6.332	16.385	−33.082	1	23.05	H
ATOM	3138	N	GLU B	169	7.44	14.052	−25.341	1	23.03	N
ATOM	3139	CA	GLU B	169	7.144	13.867	−23.922	1	27.07	C
ATOM	3140	C	GLU B	169	7.491	12.466	−23.43	1	28.35	C
ATOM	3141	O	GLU B	169	7.865	12.291	−22.271	1	29.75	O
ATOM	3142	CB	GLU B	169	5.67	14.146	−23.646	1	26.09	C
ATOM	3143	CG	GLU B	169	5.303	15.611	−23.69	1	25.97	C
ATOM	3144	CD	GLU B	169	3.812	15.826	−23.565	1	24.5	C
ATOM	3145	OE1	GLU B	169	3.374	16.389	−22.542	1	25.81	O
ATOM	3146	OE2	GLU B	169	3.078	15.423	−24.491	1	26.86	O1−
ATOM	3147	H	GLU B	169	6.762	14.294	−25.812	1	27.63	H
ATOM	3148	HA	GLU B	169	7.669	14.501	−23.408	1	32.48	H
ATOM	3149	HB2	GLU B	169	5.135	13.687	−24.312	1	31.3	H
ATOM	3150	HB3	GLU B	169	5.45	13.813	−22.762	1	31.3	H
ATOM	3151	HG2	GLU B	169	5.737	16.071	−22.954	1	31.17	H
ATOM	3152	HG3	GLU B	169	5.593	15.987	−24.536	1	31.17	H
ATOM	3153	N	ASP B	170	7.365	11.472	−24.307	1	30.2	N
ATOM	3154	CA	ASP B	170	7.651	10.088	−23.935	1	31.21	C
ATOM	3155	C	ASP B	170	9.145	9.779	−24.005	1	30.44	C
ATOM	3156	O	ASP B	170	9.549	8.62	−23.93	1	33.82	O
ATOM	3157	CB	ASP B	170	6.872	9.111	−24.827	1	31.14	C
ATOM	3158	CG	ASP B	170	7.274	9.188	−26.297	1	28.8	C
ATOM	3159	OD1	ASP B	170	8.297	9.822	−26.629	1	28.18	O
ATOM	3160	OD2	ASP B	170	6.557	8.594	−27.131	1	33.86	O1−
ATOM	3161	H	ASP B	170	7.116	11.573	−25.124	1	36.24	H
ATOM	3162	HA	ASP B	170	7.363	9.946	−23.02	1	37.45	H
ATOM	3163	HB2	ASP B	170	7.036	8.206	−24.52	1	37.37	H
ATOM	3164	HB3	ASP B	170	5.926	9.315	−24.766	1	37.37	H
ATOM	3165	N	GLY B	171	9.959	10.816	−24.173	1	28.28	N
ATOM	3166	CA	GLY B	171	11.402	10.665	−24.161	1	30.98	C
ATOM	3167	C	GLY B	171	11.999	10.269	−25.498	1	29.68	C
ATOM	3168	O	GLY B	171	13.213	10.362	−25.688	1	36.65	O
ATOM	3169	H	GLY B	171	9.693	11.625	−24.296	1	33.93	H
ATOM	3170	HA2	GLY B	171	11.806	11.503	−23.887	1	37.17	H
ATOM	3171	HA3	GLY B	171	11.644	9.987	−23.511	1	37.17	H
ATOM	3172	N	SER B	172	11.159	9.829	−26.428	1	28.25	N
ATOM	3173	CA	SER B	172	11.644	9.397	−27.733	1	32.36	C
ATOM	3174	C	SER B	172	12.201	10.584	−28.513	1	30.64	C
ATOM	3175	O	SER B	172	11.694	11.699	−28.417	1	29.69	O
ATOM	3176	CB	SER B	172	10.531	8.712	−28.527	1	30.14	C
ATOM	3177	OG	SER B	172	9.494	9.62	−28.857	1	32.1	O
ATOM	3178	H	SER B	172	10.307	9.77	−26.329	1	33.9	H
ATOM	3179	HA	SER B	172	12.362	8.757	−27.607	1	38.83	H
ATOM	3180	HB2	SER B	172	10.906	8.353	−29.346	1	36.17	H
ATOM	3181	HB3	SER B	172	10.16	7.994	−27.991	1	36.17	H
ATOM	3182	HG	SER B	172	9.158	9.939	−28.157	1	38.52	H
ATOM	3183	N	ILE B	173	13.257	10.336	−29.274	1	33.34	N
ATOM	3184	CA	ILE B	173	13.897	11.382	−30.055	1	36.79	C
ATOM	3185	C	ILE B	173	13.052	11.692	−31.284	1	34.73	C
ATOM	3186	O	ILE B	173	12.329	10.831	−31.782	1	35.37	O
ATOM	3187	CB	ILE B	173	15.328	10.966	−30.48	1	41.45	C
ATOM	3188	CG1	ILE B	173	16.111	12.158	−31.044	1	45.9	C
ATOM	3189	CG2	ILE B	173	15.285	9.821	−31.487	1	41.81	C
ATOM	3190	CD1	ILE B	173	16.543	13.16	−29.995	1	47.62	C
ATOM	3191	H	ILE B	173	13.625	9.563	−29.357	1	40.01	H
ATOM	3192	HA	ILE B	173	13.961	12.187	−29.518	1	44.15	H
ATOM	3193	HB	ILE B	173	15.794	10.65	−29.69	1	49.74	H
ATOM	3194	HG12	ILE B	173	16.91	11.826	−31.483	1	55.09	H
ATOM	3195	HG13	ILE B	173	15.553	12.623	−31.686	1	55.09	H
ATOM	3196	HG21	ILE B	173	16.193	9.584	−31.734	1	50.17	H
ATOM	3197	HG22	ILE B	173	14.843	9.06	−31.081	1	50.17	H
ATOM	3198	HG23	ILE B	173	14.794	10.11	−32.272	1	50.17	H
ATOM	3199	HD11	ILE B	173	17.029	13.879	−30.428	1	57.15	H
ATOM	3200	HD12	ILE B	173	15.755	13.513	−29.553	1	57.15	H
ATOM	3201	HD13	ILE B	173	17.114	12.715	−29.35	1	57.15	H
ATOM	3202	N	LEU B	174	13.137	12.929	−31.76	1	35.6	N
ATOM	3203	CA	LEU B	174	12.474	13.322	−32.997	1	31.48	C
ATOM	3204	C	LEU B		174	13.053	12.55	−34.174	1	35.42	C
ATOM	3205	O	LEU B	174	14.217	12.734	−34.531	1	33.32	O
ATOM	3206	CB	LEU B	174	12.623	14.826	−33.23	1	26.55	C
ATOM	3207	CG	LEU B	174	12.246	15.348	−34.619	1	31.49	C
ATOM	3208	CD1	LEU B		174	10.787	15.05	−34.937	1	27.57	C
ATOM	3209	CD2	LEU B	174	12.528	16.84	−34.714	1	29.29	C
ATOM	3210	H	LEU B		174	13.576	13.564	−31.382	1	42.72	H
ATOM	3211	HA	LEU B		174	11.528	13.116	−32.933	1	37.78	H
ATOM	3212	HB2	LEU B	174	12.063	15.289	−32.588	1	31.86	H
ATOM	3213	HB3	LEU B	174	13.551	15.065	−33.077	1	31.86	H
ATOM	3214	HG	LEU B		174	12.793	14.899	−35.282	1	37.79	H
ATOM	3215	HD11	LEU B	174	10.581	15.392	−35.821	1	33.08	H
ATOM	3216	HD12	LEU B	174	10.649	14.09	−34.913	1	33.08	H
ATOM	3217	HD13	LEU B	174	10.225	15.482	−34.275	1	33.08	H
ATOM	3218	HD21	LEU B	174	12.283	17.151	−35.599	1	35.15	H
ATOM	3219	HD22	LEU B	174	12.004	17.303	−34.043	1	35.15	H
ATOM	3220	HD23	LEU B	174	13.474	16.992	−34.56	1	35.15	H
ATOM	3221	N	SER B	175	12.242	11.686	−34.776	1	36.01	N
ATOM	3222	CA	SER B	175	12.703	10.894	−35.911	1	38.08	C
ATOM	3223	C	SER B	175	12.978	11.796	−37.114	1	39.53	C
ATOM	3224	O	SER B	175	12.257	12.771	−37.345	1	35.1	O
ATOM	3225	CB	SER B	175	11.679	9.818	−36.277	1	34.05	C
ATOM	3226	OG	SER B	175	11.435	8.952	−35.181	1	46.41	O
ATOM	3227	H	SER B	175	11.426	11.54	−34.548	1	43.22	H
ATOM	3228	HA	SER B	175	13.532	10.451	−35.672	1	45.7	H
ATOM	3229	HB2	SER B	175	10.847	10.248	−36.53	1	40.86	H
ATOM	3230	HB3	SER B	175	12.022	9.297	−37.02	1	40.86	H
ATOM	3231	HG	SER B	175	10.872	8.368	−35.397	1	55.69	H
ATOM	3232	N	PRO B	176	14.024	11.475	−37.89	1	37.56	N
ATOM	3233	CA	PRO B	176	14.394	12.331	−39.02	1	40.19	C
ATOM	3234	C	PRO B	176	13.366	12.306	−40.148	1	39.31	C
ATOM	3235	O	PRO B	176	12.536	11.398	−40.204	1	39.37	O
ATOM	3236	CB	PRO B	176	15.725	11.738	−39.482	1	42.21	C
ATOM	3237	CG	PRO B	176	15.663	10.317	−39.076	1	48.89	C
ATOM	3238	CD	PRO B	176	14.882	10.281	−37.799	1	40.78	C
ATOM	3239	HA	PRO B	176	14.53	13.245	−38.724	1	48.23	H
ATOM	3240	HB2	PRO B	176	15.803	11.818	−40.446	1	50.65	H
ATOM	3241	HB3	PRO B	176	16.459	12.192	−39.038	1	50.65	H
ATOM	3242	HG2	PRO B	176	15.212	9.803	−39.764	1	58.67	H
ATOM	3243	HG3	PRO B	176	16.562	9.981	−38.934	1	58.67	H
ATOM	3244	HD2	PRO B	176	14.341	9.477	−37.757	1	48.94	H
ATOM	3245	HD3	PRO B	176	15.478	10.35	−37.037	1	48.94	H
ATOM	3246	N	ASN B	177	13.423	13.307	−41.022	1	32.05	N
ATOM	3247	CA	ASN B	177	12.551	13.372	−42.192	1	37.49	C
ATOM	3248	C	ASN B	177	11.058	13.384	−41.853	1	32.07	C
ATOM	3249	O	ASN B	177	10.227	13.073	−42.704	1	32.22	O
ATOM	3250	CB	ASN B	177	12.853	12.2	−43.134	1	43.25	C
ATOM	3251	CG	ASN B	177	14.279	12.223	−43.656	1	42.46	C
ATOM	3252	OD1	ASN B	177	14.599	12.972	−44.579	1	48.73	O
ATOM	3253	ND2	ASN B	177	15.14	11.398	−43.072	1	42.22	N
ATOM	3254	H	ASN B	177	13.967	13.97	−40.959	1	38.46	H
ATOM	3255	HA	ASN B	177	12.746	14.191	−42.674	1	44.99	H
ATOM	3256	HB2	ASN B	177	12.722	11.367	−42.655	1	51.9	H
ATOM	3257	HB3	ASN B	177	12.253	12.243	−43.895	1	51.9	H
ATOM	3258	HD21	ASN B	177	15.959	11.376	−43.334	1	50.66	H
ATOM	3259	HD22	ASN B	177	14.879	10.886	−42.432	1	50.66	H
ATOM	3260	N	LEU B	178	10.722	13.744	−40.615	1	29.94	N
ATOM	3261	CA	LEU B	178	9.326	13.905	−40.208	1	27.52	C
ATOM	3262	C	LEU B	178	8.926	15.373	−40.174	1	28.55	C
ATOM	3263	O	LEU B	178	7.933	15.769	−40.785	1	28.18	O
ATOM	3264	CB	LEU B	178	9.082	13.284	−38.831	1	25.65	C
ATOM	3265	CG	LEU B	178	8.632	11.822	−38.77	1	29.25	C
ATOM	3266	CD1	LEU B	178	8.419	11.427	−37.326	1	30.04	C
ATOM	3267	CD2	LEU B	178	7.356	11.576	−39.57	1	30.4	C
ATOM	3268	H	LEU B	178	11.289	13.902	−39.987	1	35.93	H
ATOM	3269	HA	LEU B	178	8.755	13.452	−40.848	1	33.02	H
ATOM	3270	HB2	LEU B	178	9.907	13.346	−38.326	1	30.78	H
ATOM	3271	HB3	LEU B	178	8.398	13.808	−38.385	1	30.78	H
ATOM	3272	HG	LEU B	178	9.331	11.259	−39.137	1	35.1	H
ATOM	3273	HD11	LEU B	178	8.134	10.5	−37.292	1	36.05	H
ATOM	3274	HD12	LEU B	178	9.253	11.535	−36.844	1	36.05	H
ATOM	3275	HD13	LEU B	178	7.736	11.998	−36.94	1	36.05	H
ATOM	3276	HD21	LEU B	178	7.115	10.64	−39.499	1	36.49	H
ATOM	3277	HD22	LEU B	178	6.646	12.129	−39.209	1	36.49	H
ATOM	3278	HD23	LEU B	178	7.517	11.808	−40.498	1	36.49	H
ATOM	3279	N	LEU B	179	9.706	16.171	−39.449	1	24.55	N
ATOM	3280	CA	LEU B	179	9.42	17.591	−39.277	1	21.87	C
ATOM	3281	C	LEU B	179	10.57	18.473	−39.737	1	24.32	C
ATOM	3282	O	LEU B	179	11.735	18.189	−39.457	1	23.82	O
ATOM	3283	CB	LEU B	179	9.114	17.896	−37.81	1	23.91	C
ATOM	3284	CG	LEU B		179	7.814	17.348	−37.224	1	22.72	C
ATOM	3285	CD1	LEU B	179	7.76	17.633	−35.726	1	20.68	C
ATOM	3286	CD2	LEU B	179	6.602	17.946	−37.927	1	23.32	C
ATOM	3287	H	LEU B	179	10.416	15.909	−39.041	1	29.47	H
ATOM	3288	HA	LEU B		179	8.637	17.821	−39.802	1	26.24	H
ATOM	3289	HB2	LEU B	179	9.839	17.539	−37.273	1	28.7	H
ATOM	3290	HB3	LEU B	179	9.088	18.86	−37.705	1	28.7	H
ATOM	3291	HG	LEU B		179	7.791	16.387	−37.349	1	27.27	H
ATOM	3292	HD11	LEU B	179	6.931	17.28	−35.368	1	24.81	H
ATOM	3293	HD12	LEU B	179	8.516	17.203	−35.296	1	24.81	H
ATOM	3294	HD13	LEU B	179	7.8	18.592	−35.586	1	24.81	H
ATOM	3295	HD21	LEU B	179	5.795	17.579	−37.533	1	27.98	H
ATOM	3296	HD22	LEU B	179	6.616	18.91	−37.816	1	27.98	H
ATOM	3297	HD23	LEU B	179	6.642	17.721	−38.87	1	27.98	H
ATOM	3298	N	THR B	180	10.228	19.547	−40.441	1	21.44	N
ATOM	3299	CA	THR B	180	11.169	20.621	−40.726	1	24.48	C
ATOM	3300	C	THR B	180	11.15	21.596	−39.556	1	24.18	C
ATOM	3301	O	THR B	180	10.148	22.277	−39.33	1	20.49	O
ATOM	3302	CB	THR B	180	10.814	21.367	−42.029	1	26.75	C
ATOM	3303	OG1	THR B	180	10.749	20.439	−43.119	1	26.99	O
ATOM	3304	CG2	THR B	180	11.848	22.444	−42.342	1	29.06	C
ATOM	3305	H	THR B	180	9.444	19.678	−40.769	1	25.72	H
ATOM	3306	HA	THR B	180	12.063	20.256	−40.812	1	29.38	H
ATOM	3307	HB	THR B	180	9.951	21.798	−41.926	1	32.1	H
ATOM	3308	HG1	THR B	180	10.161	19.858	−42.966	1	32.39	H
ATOM	3309	HG21	THR B	180	11.611	22.903	−43.163	1	34.88	H
ATOM	3310	HG22	THR B	180	11.883	23.09	−41.619	1	34.88	H
ATOM	3311	HG23	THR B	180	12.724	22.041	−42.448	1	34.88	H
ATOM	3312	N	ILE B	181	12.246	21.645	−38.804	1	23.05	N
ATOM	3313	CA	ILE B	181	12.353	22.54	−37.656	1	22.09	C
ATOM	3314	C	ILE B	181	12.91	23.895	−38.081	1	26.12	C
ATOM	3315	O	ILE B	181	13.964	23.972	−38.711	1	23.5	O
ATOM	3316	CB	ILE B	181	13.251	21.948	−36.557	1	23.97	C
ATOM	3317	CG1	ILE B	181	12.745	20.565	−36.131	1	23.66	C
ATOM	3318	CG2	ILE B	181	13.312	22.885	−35.356	1	22.95	C
ATOM	3319	CD1	ILE B	181	11.326	20.552	−35.592	1	28.66	C
ATOM	3320	H	ILE B	181	12.947	21.167	−38.94	1	27.67	H
ATOM	3321	HA	ILE B	181	11.47	22.681	−37.281	1	26.51	H
ATOM	3322	HB	ILE B	181	14.147	21.849	−36.914	1	28.77	H
ATOM	3323	HG12	ILE B	181	12.773	19.974	−36.899	1	28.39	H
ATOM	3324	HG13	ILE B	181	13.327	20.223	−35.434	1	28.39	H
ATOM	3325	HG21	ILE B	181	13.883	22.492	−34.677	1	27.55	H
ATOM	3326	HG22	ILE B	181	13.676	23.738	−35.64	1	27.55	H
ATOM	3327	HG23	ILE B	181	12.416	23.008	−35.005	1	27.55	H
ATOM	3328	HD11	ILE B	181	11.089	19.643	−35.348	1	34.39	H
ATOM	3329	HD12	ILE B	181	11.279	21.126	−34.812	1	34.39	H
ATOM	3330	HD13	ILE B	181	10.724	20.877	−36.279	1	34.39	H
ATOM	3331	N	ILE B	182	12.203	24.958	−37.706	1	23.73	N
ATOM	3332	CA	ILE B	182	12.514	26.304	−38.171	1	20.26	C
ATOM	3333	C	ILE B	182	12.68	27.254	−36.992	1	23.35	C
ATOM	3334	O	ILE B	182	11.782	27.378	−36.163	1	18.77	O
ATOM	3335	CB	ILE B	182	11.4	26.838	−39.101	1	21.54	C
ATOM	3336	CG1	ILE B	182	11.154	25.858	−40.255	1	22.95	C
ATOM	3337	CG2	ILE B	182	11.751	28.23	−39.631	1	20.67	C
ATOM	3338	CD1	ILE B	182	9.889	26.137	−41.035	1	27.62	C
ATOM	3339	H	ILE B	182	11.528	24.923	−37.174	1	28.48	H
ATOM	3340	HA	ILE B	182	13.346	26.287	−38.669	1	24.31	H
ATOM	3341	HB	ILE B	182	10.582	26.908	−38.585	1	25.85	H
ATOM	3342	HG12	ILE B	182	11.9	25.909	−40.873	1	27.54	H
ATOM	3343	HG13	ILE B	182	11.087	24.96	−39.894	1	27.54	H
ATOM	3344	HG21	ILE B	182	11.036	28.537	−40.21	1	24.8	H
ATOM	3345	HG22	ILE B	182	11.854	28.836	−38.881	1	24.8	H
ATOM	3346	HG23	ILE B	182	12.581	28.177	−40.13	1	24.8	H
ATOM	3347	HD11	ILE B	182	9.803	25.48	−41.743	1	33.14	H
ATOM	3348	HD12	ILE B	182	9.129	26.078	−40.435	1	33.14	H
ATOM	3349	HD13	ILE B	182	9.942	27.028	−41.415	1	33.14	H
ATOM	3350	N	GLU B	183	13.821	27.934	−36.916	1	24.54	N
ATOM	3351	CA	GLU B	183	14.022	28.911	−35.854	1	27.28	C
ATOM	3352	C	GLU B	183	13.14	30.122	−36.128	1	29.16	C
ATOM	3353	O	GLU B	183	13.045	30.599	−37.26	1	34.53	O
ATOM	3354	CB	GLU B	183	15.494	29.314	−35.73	1	36.17	C
ATOM	3355	CG	GLU B	183	16.063	30.065	−36.915	1	45.13	C
ATOM	3356	CD	GLU B	183	17.553	30.328	−36.767	1	52.61	C
ATOM	3357	OE1	GLU B	183	18.036	30.396	−35.616	1	55.37	O
ATOM	3358	OE2	GLU B	183	18.243	30.456	−37.8	1	57.38	O1−
ATOM	3359	H	GLU B	183	14.482	27.851	−37.459	1	29.44	H
ATOM	3360	HA	GLU B	183	13.745	28.522	−35.01	1	32.74	H
ATOM	3361	HB2	GLU B	183	15.592	29.882	−34.95	1	43.4	H
ATOM	3362	HB3	GLU B	183	16.024	28.51	−35.613	1	43.4	H
ATOM	3363	HG2	GLU B	183	15.927	29.54	−37.719	1	54.15	H
ATOM	3364	HG3	GLU B	183	15.612	30.92	−36.995	1	54.15	H
ATOM	3365	N	MET B	184	12.478	30.594	−35.08	1	29.01	N
ATOM	3366	CA	MET B	184	11.478	31.648	−35.192	1	25.24	C
ATOM	3367	C	MET B	184	11.643	32.571	−33.986	1	34.39	C
ATOM	3368	O	MET B	184	11.916	33.764	−34.133	1	34.16	O
ATOM	3369	CB	MET B	184	10.075	31.032	−35.263	1	25.23	C
ATOM	3370	CG	MET B	184	8.947	31.974	−35.675	1	22.62	C
ATOM	3371	SD	MET B	184	8.098	32.757	−34.293	1	34.48	S
ATOM	3372	CE	MET B	184	7.45	31.341	−33.4	1	28.01	C
ATOM	3373	H	MET B	184	12.592	30.314	−34.275	1	34.81	H
ATOM	3374	HA	MET B	184	11.631	32.152	−36.006	1	30.28	H
ATOM	3375	HB2	MET B	184	10.093	30.305	−35.905	1	30.28	H
ATOM	3376	HB3	MET B	184	9.852	30.681	−34.386	1	30.28	H
ATOM	3377	HG2	MET B	184	9.317	32.677	−36.231	1	27.15	H
ATOM	3378	HG3	MET B	184	8.289	31.47	−36.179	1	27.15	H
ATOM	3379	HE1	MET B	184	6.964	31.655	−32.621	1	33.61	H
ATOM	3380	HE2	MET B	184	6.855	30.845	−33.984	1	33.61	H
ATOM	3381	HE3	MET B	184	8.189	30.777	−33.124	1	33.61	H
ATOM	3382	N	GLN B	185	11.505	31.998	−32.794	1	32.9	N
ATOM	3383	CA	GLN B	185	11.808	32.696	−31.549	1	32.39	C
ATOM	3384	C	GLN B	185	12.769	31.85	−30.723	1	34.72	C
ATOM	3385	O	GLN B	185	12.721	30.619	−30.769	1	28.22	O
ATOM	3386	CB	GLN B	185	10.531	32.976	−30.754	1	29.62	C
ATOM	3387	CG	GLN B	185	9.601	34	−31.39	1	33.22	C
ATOM	3388	CD	GLN B	185	9.964	35.435	−31.046	1	40.19	C
ATOM	3389	OE1	GLN B	185	11.094	35.73	−30.652	1	41.44	O
ATOM	3390	NE2	GLN B	185	8.997	36.337	−31.188	1	34.22	N
ATOM	3391	H	GLN B	185	11.232	31.19	−32.679	1	39.48	H
ATOM	3392	HA	GLN B	185	12.237	33.542	−31.749	1	38.87	H
ATOM	3393	HB2	GLN B	185	10.036	32.148	−30.659	1	35.55	H
ATOM	3394	HB3	GLN B	185	10.779	33.31	−29.877	1	35.55	H
ATOM	3395	HG2	GLN B	185	9.641	33.905	−32.355	1	39.87	H
ATOM	3396	HG3	GLN B	185	8.696	33.839	−31.08	1	39.87	H
ATOM	3397	HE21	GLN B	185	9.15	37.164	−31.007	1	41.06	H
ATOM	3398	HE22	GLN B	185	8.218	36.094	−31.461	1	41.06	H
ATOM	3399	N	LYS B	186	13.654	32.506	−29.98	1	34.85	N
ATOM	3400	CA	LYS B	186	14.542	31.796	−29.071	1	34.85	C
ATOM	3401	C	LYS B	186	13.694	31.086	−28.016	1	28.04	C
ATOM	3402	O	LYS B	186	12.924	31.726	−27.301	1	27.27	O
ATOM	3403	CB	LYS B	186	15.533	32.763	−28.418	1	43.85	C
ATOM	3404	CG	LYS B	186	16.859	32.136	−28.014	1	64.98	C
ATOM	3405	CD	LYS B	186	17.666	31.694	−29.229	1	85.87	C
ATOM	3406	CE	LYS B	186	19.083	31.299	−28.845	1	104.79	C
ATOM	3407	NZ	LYS B	186	19.756	30.516	−29.918	1	110.38	N1+
ATOM	3408	H	LYS B	186	13.758	33.359	−29.984	1	41.82	H
ATOM	3409	HA	LYS B	186	15.043	31.127	−29.563	1	41.82	H
ATOM	3410	HB2	LYS B	186	15.725	33.478	−29.044	1	52.62	H
ATOM	3411	HB3	LYS B	186	15.125	33.13	−27.618	1	52.62	H
ATOM	3412	HG2	LYS B	186	17.383	32.788	−27.523	1	77.98	H
ATOM	3413	HG3	LYS B	186	16.69	31.357	−27.462	1	77.98	H
ATOM	3414	HD2	LYS B		186	17.236	30.925	−29.635	1	103.05	H
ATOM	3415	HD3	LYS B	186	17.716	32.425	−29.864	1	103.05	H
ATOM	3416	HE2	LYS B	186	19.604	32.101	−28.684	1	125.75	H
ATOM	3417	HE3	LYS B	186	19.055	30.753	−28.044	1	125.75	H
ATOM	3418	HZ1	LYS B	186	19.799	30.999	−30.664	1	132.46	H
ATOM	3419	HZ2	LYS B	186	20.581	30.301	−29.664	1	132.46	H
ATOM	3420	HZ3	LYS B	186	19.3	29.77	−30.081	1	132.46	H
ATOM	3421	N	GLY B	187	13.816	29.765	−27.932	1	25.29	N
ATOM	3422	CA	GLY B	187	13.002	28.997	−27.007	1	25.76	C
ATOM	3423	C	GLY B	187	13.264	27.506	−27.086	1	23.48	C
ATOM	3424	O	GLY B	187	14.02	27.05	−27.944	1	19.67	O
ATOM	3425	H	GLY B	187	14.362	29.294	−28.4	1	30.35	H
ATOM	3426	HA2	GLY B	187	13.181	29.291	−26.101	1	30.91	H
ATOM	3427	HA3	GLY B	187	12.064	29.152	−27.2	1	30.91	H
ATOM	3428	N	ASP B	188	12.629	26.752	−26.19	1	17.61	N
ATOM	3429	CA	ASP B	188	12.873	25.316	−26.064	1	20.1	C
ATOM	3430	C	ASP B	188	11.623	24.472	−26.317	1	17.87	C
ATOM	3431	O	ASP B	188	11.587	23.291	−25.973	1	18.91	O
ATOM	3432	CB	ASP B	188	13.42	25	−24.673	1	22.84	C
ATOM	3433	CG	ASP B	188	14.737	25.686	−24.393	1	27	C
ATOM	3434	OD1	ASP B	188	15.629	25.638	−25.265	1	28.51	O
ATOM	3435	OD2	ASP B	188	14.877	26.274	−23.3	1	29.6	O1−
ATOM	3436	H	ASP B	188	12.044	27.053	−25.637	1	21.13	H
ATOM	3437	HA	ASP B	188	13.544	25.055	−26.714	1	24.12	H
ATOM	3438	HB2	ASP B	188	12.78	25.296	−24.007	1	27.41	H
ATOM	3439	HB3	ASP B	188	13.559	24.043	−24.598	1	27.41	H
ATOM	3440	N	CYS B	189	10.597	25.079	−26.901	1	15.55	N
ATOM	3441	CA	CYS B	189	9.399	24.344	−27.293	1	18.29	C
ATOM	3442	C	CYS B	189	9.129	24.575	−28.777	1	18.34	C
ATOM	3443	O	CYS B	189	9.771	25.421	−29.403	1	16.24	O
ATOM	3444	CB	CYS B	189	8.202	24.763	−26.437	1	21.42	C
ATOM	3445	SG	CYS B	189	8.369	24.31	−24.685	1	19.88	S
ATOM	3446	H	CYS B	189	10.568	25.919	−27.083	1	18.66	H
ATOM	3447	HA	CYS B	189	9.549	23.395	−27.158	1	21.95	H
ATOM	3448	HB2	CYS B	189	8.103	25.726	−26.487	1	25.71	H
ATOM	3449	HB3	CYS B	189	7.404	24.331	−26.781	1	25.71	H
ATOM	3450	N	ALA B	190	8.195	23.813	−29.337	1	17.84	N
ATOM	3451	CA	ALA B	190	7.935	23.856	−30.773	1	16.98	C
ATOM	3452	C	ALA B	190	6.443	23.85	−31.098	1	13.84	C
ATOM	3453	O	ALA B	190	5.68	23.04	−30.566	1	13.74	O
ATOM	3454	CB	ALA B	190	8.622	22.686	−31.461	1	18.2	C
ATOM	3455	H	ALA B	190	7.697	23.26	−28.907	1	21.4	H
ATOM	3456	HA	ALA B	190	8.312	24.674	−31.133	1	20.37	H
ATOM	3457	HB1	ALA B	190	8.44	22.729	−32.413	1	21.84	H
ATOM	3458	HB2	ALA B	190	9.577	22.744	−31.303	1	21.84	H
ATOM	3459	HB3	ALA B	190	8.275	21.858	−31.094	1	21.84	H
ATOM	3460	N	LEU B	191	6.047	24.763	−31.982	1	11.45	N
ATOM	3461	CA	LEU B	191	4.68	24.829	−32.492	1	14.13	C
ATOM	3462	C	LEU B	191	4.554	23.994	−33.749	1	16.78	C
ATOM	3463	O	LEU B	191	5.395	24.1	−34.642	1	15.41	O
ATOM	3464	CB	LEU B	191	4.288	26.269	−32.817	1	12.09	C
ATOM	3465	CG	LEU B	191	4.165	27.255	−31.659	1	14.17	C
ATOM	3466	CD1	LEU B	191	4.052	28.666	−32.203	1	14.01	C
ATOM	3467	CD2	LEU B	191	2.958	26.915	−30.798	1	16.56	C
ATOM	3468	H	LEU B	191	6.564	25.368	−32.309	1	13.74	H
ATOM	3469	HA	LEU B	191	4.066	24.482	−31.825	1	16.96	H
ATOM	3470	HB2	LEU B	191	4.953	26.629	−33.424	1	14.51	H
ATOM	3471	HB3	LEU B	191	3.428	26.25	−33.264	1	14.51	H
ATOM	3472	HG	LEU B	191	4.959	27.203	−31.105	1	17.01	H
ATOM	3473	HD11	LEU B	191	3.974	29.285	−31.461	1	16.81	H
ATOM	3474	HD12	LEU B	191	4.847	28.868	−32.721	1	16.81	H
ATOM	3475	HD13	LEU B	191	3.265	28.724	−32.768	1	16.81	H
ATOM	3476	HD21	LEU B	191	2.9	27.553	−30.07	1	19.87	H
ATOM	3477	HD22	LEU B	191	2.158	26.962	−31.345	1	19.87	H
ATOM	3478	HD23	LEU B	191	3.065	26.018	−30.445	1	19.87	H
ATOM	3479	N	TYR B	192	3.513	23.172	−33.834	1	16.15	N
ATOM	3480	CA	TYR B	192	3.244	22.485	−35.084	1	12.87	C
ATOM	3481	C	TYR B	192	2.607	23.44	−36.076	1	18.63	C
ATOM	3482	O	TYR B	192	1.704	24.209	−35.732	1	14.22	O
ATOM	3483	CB	TYR B	192	2.322	21.279	−34.921	1	17.45	C
ATOM	3484	CG	TYR B	192	2.041	20.673	−36.28	1	18.09	C
ATOM	3485	CD1	TYR B	192	2.958	19.818	−36.876	1	18.3	C
ATOM	3486	CD2	TYR B	192	0.901	21.013	−36.997	1	15.77	C
ATOM	3487	CE1	TYR B	192	2.731	19.287	−38.131	1	17.41	C
ATOM	3488	CE2	TYR B	192	0.666	20.487	−38.257	1	19.17	C
ATOM	3489	CZ	TYR B	192	1.586	19.625	−38.819	1	19.87	C
ATOM	3490	OH	TYR B	192	1.361	19.098	−40.072	1	20.58	O
ATOM	3491	H	TYR B	192	2.962	22.999	−33.197	1	19.37	H
ATOM	3492	HA	TYR B	192	4.082	22.174	−35.461	1	15.44	H
ATOM	3493	HB2	TYR B	192	2.753	20.611	−34.366	1	20.94	H
ATOM	3494	HB3	TYR B	192	1.482	21.561	−34.527	1	20.94	H
ATOM	3495	HD1	TYR B	192	3.734	19.589	−36.417	1	21.96	H
ATOM	3496	HD2	TYR B	192	0.281	21.595	−36.621	1	18.92	H
ATOM	3497	HE1	TYR B	192	3.351	18.706	−38.512	1	20.89	H
ATOM	3498	HE2	TYR B	192	−0.107	20.714	−38.722	1	23	H
ATOM	3499	HH	TYR B	192	0.633	19.384	−40.377	1	24.69	H
ATOM	3500	N	ALA B	193	3.077	23.36	−37.315	1	12.79	N
ATOM	3501	CA	ALA B	193	2.483	24.079	−38.431	1	15.94	C
ATOM	3502	C	ALA B	193	2.55	23.173	−39.65	1	18.77	C
ATOM	3503	O	ALA B	193	3.498	22.402	−39.801	1	16.34	O
ATOM	3504	CB	ALA B	193	3.211	25.385	−38.685	1	17.09	C
ATOM	3505	H	ALA B	193	3.756	22.883	−37.538	1	15.35	H
ATOM	3506	HA	ALA B	193	1.553	24.274	−38.238	1	19.13	H
ATOM	3507	HB1	ALA B	193	2.792	25.839	−39.433	1	20.5	H
ATOM	3508	HB2	ALA B	193	3.156	25.937	−37.89	1	20.5	H
ATOM	3509	HB3	ALA B	193	4.139	25.194	−38.892	1	20.5	H
ATOM	3510	N	SER B	194	1.543	23.243	−40.509	1	15.79	N
ATOM	3511	CA	SER B	194	1.535	22.414	−41.708	1	21.22	C
ATOM	3512	C	SER B	194	2.354	23.092	−42.803	1	20.82	C
ATOM	3513	O	SER B	194	2.449	24.317	−42.813	1	23.78	O
ATOM	3514	CB	SER B	194	0.109	22.172	−42.191	1	20.14	C
ATOM	3515	OG	SER B	194	−0.41	23.338	−42.795	1	26.86	O
ATOM	3516	H	SER B	194	0.859	23.757	−40.424	1	18.95	H
ATOM	3517	HA	SER B	194	1.941	21.555	−41.509	1	25.47	H
ATOM	3518	HB2	SER B	194	0.113	21.453	−42.842	1	24.17	H
ATOM	3519	HB3	SER B	194	−0.446	21.933	−41.433	1	24.17	H
ATOM	3520	HG	SER B	194	−0.416	23.97	−42.241	1	32.23	H
ATOM	3521	N	SER B	195	2.948	22.328	−43.72	1	22.26	N
ATOM	3522	CA	SER B	195	2.901	20.869	−43.738	1	19.41	C
ATOM	3523	C	SER B	195	4.097	20.267	−42.993	1	26.14	C
ATOM	3524	O	SER B	195	5.234	20.349	−43.461	1	25.77	O
ATOM	3525	CB	SER B	195	2.879	20.368	−45.182	1	28.07	C
ATOM	3526	OG	SER B	195	2.594	18.984	−45.234	1	34.28	O
ATOM	3527	H	SER B	195	3.406	22.652	−44.372	1	26.71	H
ATOM	3528	HA	SER B	195	2.089	20.571	−43.3	1	23.3	H
ATOM	3529	HB2	SER B	195	2.194	20.849	−45.672	1	33.69	H
ATOM	3530	HB3	SER B	195	3.747	20.527	−45.584	1	33.69	H
ATOM	3531	HG	SER B	195	3.18	18.555	−44.813	1	41.13	H
ATOM	3532	N	PHE B	196	3.832	19.674	−41.832	1	24.04	N
ATOM	3533	CA	PHE B	196	4.858	19	−41.029	1	22.02	C
ATOM	3534	C	PHE B	196	6.07	19.879	−40.731	1	23.97	C
ATOM	3535	O	PHE B	196	7.214	19.502	−40.988	1	20.66	O
ATOM	3536	CB	PHE B	196	5.297	17.709	−41.724	1	24	C
ATOM	3537	CG	PHE B	196	4.251	16.638	−41.695	1	22.78	C
ATOM	3538	CD1	PHE B	196	4.128	15.806	−40.596	1	23.64	C
ATOM	3539	CD2	PHE B	196	3.373	16.477	−42.751	1	28.16	C
ATOM	3540	CE1	PHE B	196	3.156	14.827	−40.556	1	24.03	C
ATOM	3541	CE2	PHE B	196	2.399	15.5	−42.716	1	29.08	C
ATOM	3542	CZ	PHE B	196	2.288	14.675	−41.617	1	25.46	C
ATOM	3543	H	PHE B	196	3.048	19.646	−41.479	1	28.84	H
ATOM	3544	HA	PHE B	196	4.465	18.752	−40.178	1	26.42	H
ATOM	3545	HB2	PHE B	196	5.499	17.904	−42.652	1	28.8	H
ATOM	3546	HB3	PHE B	196	6.088	17.366	−41.279	1	28.8	H
ATOM	3547	HD1	PHE B	196	4.709	15.907	−39.877	1	28.37	H
ATOM	3548	HD2	PHE B	196	3.44	17.033	−43.493	1	33.8	H
ATOM	3549	HE1	PHE B	196	3.086	14.271	−39.814	1	28.83	H
ATOM	3550	HE2	PHE B	196	1.817	15.398	−43.434	1	34.9	H
ATOM	3551	HZ	PHE B	196	1.635	14.013	−41.594	1	30.55	H
ATOM	3552	N	LYS B	197	5.795	21.056	−40.182	1	23.08	N
ATOM	3553	CA	LYS B	197	6.829	21.97	−39.726	1	20.49	C
ATOM	3554	C	LYS B	197	6.749	22.119	−38.22	1	18.79	C
ATOM	3555	O	LYS B	197	5.683	21.951	−37.624	1	16.31	O
ATOM	3556	CB	LYS B	197	6.681	23.346	−40.376	1	23.24	C
ATOM	3557	CG	LYS B	197	6.695	23.349	−41.889	1	26.94	C
ATOM	3558	CD	LYS B	197	6.409	24.749	−42.412	1	35.07	C
ATOM	3559	CE	LYS B	197	6.323	24.784	−43.924	1	45.32	C
ATOM	3560	NZ	LYS B	197	6.012	26.155	−44.422	1	56.39	N1+
ATOM	3561	H	LYS B	197	4.998	21.354	−40.061	1	27.7	H
ATOM	3562	HA	LYS B	197	7.702	21.613	−39.955	1	24.58	H
ATOM	3563	HB2	LYS B	197	5.838	23.731	−40.092	1	27.89	H
ATOM	3564	HB3	LYS B	197	7.412	23.908	−40.077	1	27.89	H
ATOM	3565	HG2	LYS B	197	7.57	23.074	−42.205	1	32.33	H
ATOM	3566	HG3	LYS B	197	6.009	22.749	−42.221	1	32.33	H
ATOM	3567	HD2	LYS B	197	5.561	25.056	−42.054	1	42.09	H
ATOM	3568	HD3	LYS B	197	7.123	25.345	−42.135	1	42.09	H
ATOM	3569	HE2	LYS B	197	7.175	24.51	−44.299	1	54.39	H
ATOM	3570	HE3	LYS B	197	5.619	24.186	−44.218	1	54.39	H
ATOM	3571	HZ1	LYS B	197	5.967	26.152	−45.311	1	67.66	H
ATOM	3572	HZ2	LYS B	197	5.231	26.428	−44.094	1	67.66	H
ATOM	3573	HZ3	LYS B	197	6.648	26.723	−44.167	1	67.66	H
ATOM	3574	N	GLY B	198	7.886	22.439	−37.617	1	17.88	N
ATOM	3575	CA	GLY B	198	7.954	22.804	−36.219	1	15.29	C
ATOM	3576	C	GLY B	198	8.632	24.154	−36.088	1	16.13	C
ATOM	3577	O	GLY B	198	9.783	24.311	−36.488	1	18.89	O
ATOM	3578	H	GLY B	198	8.65	22.452	−38.012	1	21.46	H
ATOM	3579	HA2	GLY B	198	7.061	22.86	−35.845	1	18.34	H
ATOM	3580	HA3	GLY B	198	8.465	22.143	−35.726	1	18.34	H
ATOM	3581	N	TYR B	199	7.914	25.136	−35.554	1	16	N
ATOM	3582	CA	TYR B	199	8.489	26.452	−35.299	1	17.75	C
ATOM	3583	C	TYR B	199	8.943	26.544	−33.849	1	19.24	C
ATOM	3584	O	TYR B	199	8.155	26.33	−32.932	1	16.43	O
ATOM	3585	CB	TYR B	199	7.481	27.562	−35.6	1	15.65	C
ATOM	3586	CG	TYR B	199	7.254	27.819	−37.072	1	15.66	C
ATOM	3587	CD1	TYR B	199	8.128	28.612	−37.801	1	17.35	C
ATOM	3588	CD2	TYR B	199	6.151	27.285	−37.728	1	22.19	C
ATOM	3589	CE1	TYR B	199	7.918	28.856	−39.15	1	24.18	C
ATOM	3590	CE2	TYR B	199	5.931	27.523	−39.074	1	19.74	C
ATOM	3591	CZ	TYR B	199	6.817	28.308	−39.78	1	27.19	C
ATOM	3592	OH	TYR B	199	6.6	28.545	−41.117	1	25.4	O
ATOM	3593	H	TYR B	199	7.087	25.065	−35.329	1	19.2	H
ATOM	3594	HA	TYR B	199	9.262	26.58	−35.869	1	21.3	H
ATOM	3595	HB2	TYR B	199	6.628	27.321	−35.208	1	18.77	H
ATOM	3596	HB3	TYR B	199	7.801	28.387	−35.204	1	18.77	H
ATOM	3597	HD1	TYR B	199	8.871	28.981	−37.38	1	20.82	H
ATOM	3598	HD2	TYR B	199	5.552	26.754	−37.255	1	26.63	H
ATOM	3599	HE1	TYR B	199	8.515	29.386	−39.628	1	29.02	H
ATOM	3600	HE2	TYR B	199	5.191	27.155	−39.499	1	23.69	H
ATOM	3601	HH	TYR B	199	7.209	29.034	−41.425	1	30.48	H
ATOM	3602	N	ILE B	200	10.218	26.861	−33.648	1	18.78	N
ATOM	3603	CA	ILE B	200	10.764	27.005	−32.305	1	20.57	C
ATOM	3604	C	ILE B	200	10.151	28.24	−31.654	1	22.09	C
ATOM	3605	O	ILE B	200	10.139	29.323	−32.242	1	21.41	O
ATOM	3606	CB	ILE B	200	12.305	27.118	−32.322	1	22.56	C
ATOM	3607	CG1	ILE B	200	12.914	25.902	−33.023	1	23.09	C
ATOM	3608	CG2	ILE B	200	12.85	27.236	−30.901	1	23.03	C
ATOM	3609	CD1	ILE B	200	14.406	26.001	−33.258	1	28.91	C
ATOM	3610	H	ILE B	200	10.789	26.998	−34.276	1	22.53	H
ATOM	3611	HA	ILE B	200	10.522	26.229	−31.775	1	24.68	H
ATOM	3612	HB	ILE B	200	12.551	27.916	−32.816	1	27.07	H
ATOM	3613	HG12	ILE B	200	12.753	25.116	−32.478	1	27.71	H
ATOM	3614	HG13	ILE B	200	12.486	25.794	−33.887	1	27.71	H
ATOM	3615	HG21	ILE B	200	13.816	27.306	−30.939	1	27.64	H
ATOM	3616	HG22	ILE B	200	12.476	28.029	−30.485	1	27.64	H
ATOM	3617	HG23	ILE B	200	12.594	26.447	−30.399	1	27.64	H
ATOM	3618	HD11	ILE B	200	14.709	25.194	−33.704	1	34.69	H
ATOM	3619	HD12	ILE B	200	14.587	26.775	−33.814	1	34.69	H
ATOM	3620	HD13	ILE B	200	14.854	26.095	−32.403	1	34.69	H
ATOM	3621	N	GLU B	201	9.629	28.066	−30.445	1	18.17	N
ATOM	3622	CA	GLU B	201	8.939	29.143	−29.751	1	18.13	C
ATOM	3623	C	GLU B	201	9.234	29.096	−28.26	1	19.85	C
ATOM	3624	O	GLU B	201	9.528	28.034	−27.703	1	17.15	O
ATOM	3625	CB	GLU B	201	7.428	29.05	−30.006	1	16.42	C
ATOM	3626	CG	GLU B	201	6.564	30.052	−29.239	1	24.81	C
ATOM	3627	CD	GLU B	201	6.879	31.502	−29.577	1	29.39	C
ATOM	3628	OE1	GLU B	201	7.969	31.986	−29.202	1	28.55	O
ATOM	3629	OE2	GLU B	201	6.028	32.161	−30.213	1	33.83	O1−
ATOM	3630	H	GLU B	201	9.663	27.329	−30.003	1	21.8	H
ATOM	3631	HA	GLU B	201	9.251	29.994	−30.094	1	21.75	H
ATOM	3632	HB2	GLU B	201	7.268	29.193	−30.952	1	19.7	H
ATOM	3633	HB3	GLU B	201	7.13	28.161	−29.759	1	19.7	H
ATOM	3634	HG2	GLU B	201	5.632	29.892	−29.453	1	29.77	H
ATOM	3635	HG3	GLU B	201	6.71	29.929	−28.288	1	29.77	H
ATOM	3636	N	ASN B	202	9.168	30.26	−27.625	1	21.76	N
ATOM	3637	CA	ASN B	202	9.292	30.361	−26.179	1	22.4	C
ATOM	3638	C	ASN B	202	8.163	29.592	−25.495	1	18.61	C
ATOM	3639	O	ASN B	202	6.984	29.863	−25.726	1	17.6	O
ATOM	3640	CB	ASN B	202	9.284	31.831	−25.75	1	25.89	C
ATOM	3641	CG	ASN B	202	9.627	32.019	−24.284	1	30.35	C
ATOM	3642	OD1	ASN B	202	9.134	31.298	−23.417	1	28.07	O
ATOM	3643	ND2	ASN B	202	10.484	32.995	−24.002	1	32.66	N
ATOM	3644	H	ASN B	202	9.049	31.017	−28.017	1	26.11	H
ATOM	3645	HA	ASN B	202	10.135	29.969	−25.904	1	26.88	H
ATOM	3646	HB2	ASN B	202	9.938	32.317	−26.276	1	31.07	H
ATOM	3647	HB3	ASN B	202	8.399	32.199	−25.9	1	31.07	H
ATOM	3648	HD21	ASN B	202	10.713	33.144	−23.187	1	39.19	H
ATOM	3649	HD22	ASN B	202	10.81	33.477	−24.635	1	39.19	H
ATOM	3650	N	CYS B	203	8.541	28.633	−24.654	1	15.24	N
ATOM	3651	CA	CYS B	203	7.584	27.779	−23.962	1	18.87	C
ATOM	3652	C	CYS B	203	6.517	28.573	−23.207	1	18.33	C
ATOM	3653	O	CYS B	203	5.426	28.065	−22.954	1	20.66	O
ATOM	3654	CB	CYS B	203	8.322	26.852	−22.989	1	18.37	C
ATOM	3655	SG	CYS B	203	9.514	25.728	−23.774	1	24.48	S
ATOM	3656	H	CYS B	203	9.361	28.456	−24.465	1	18.29	H
ATOM	3657	HA	CYS B	203	7.132	27.223	−24.615	1	22.64	H
ATOM	3658	HB2	CYS B	203	8.809	27.397	−22.351	1	22.04	H
ATOM	3659	HB3	CYS B	203	7.668	26.309	−22.522	1	22.04	H
ATOM	3660	N	SER B	204	6.83	29.819	−22.859	1	17.86	N
ATOM	3661	CA	SER B	204	5.916	30.656	−22.087	1	22.5	C
ATOM	3662	C	SER B	204	4.864	31.354	−22.948	1	20.68	C
ATOM	3663	O	SER B	204	3.937	31.963	−22.42	1	22.63	O
ATOM	3664	CB	SER B	204	6.703	31.71	−21.302	1	20.13	C
ATOM	3665	OG	SER B	204	7.47	31.104	−20.279	1	22.97	O
ATOM	3666	H	SER B	204	7.571	30.206	−23.061	1	21.43	H
ATOM	3667	HA	SER B	204	5.449	30.098	−21.446	1	27	H
ATOM	3668	HB2	SER B	204	7.298	32.177	−21.909	1	24.15	H
ATOM	3669	HB3	SER B	204	6.08	32.335	−20.901	1	24.15	H
ATOM	3670	HG	SER B	204	7.898	31.69	−19.855	1	27.57	H
ATOM	3671	N	THR B	205	5.005	31.27	−24.267	1	18.95	N
ATOM	3672	CA	THR B	205	4.096	31.964	−25.178	1	19.15	C
ATOM	3673	C	THR B	205	2.756	31.236	−25.307	1	18.16	C
ATOM	3674	O	THR B	205	2.722	30.073	−25.709	1	16.01	O
ATOM	3675	CB	THR B	205	4.704	32.103	−26.585	1	25.38	C
ATOM	3676	OG1	THR B	205	6.06	32.554	−26.487	1	28.77	O
ATOM	3677	CG2	THR B	205	3.896	33.092	−27.42	1	24.93	C
ATOM	3678	H	THR B	205	5.621	30.817	−24.661	1	22.74	H
ATOM	3679	HA	THR B	205	3.924	32.855	−24.835	1	22.99	H
ATOM	3680	HB	THR B	205	4.684	31.241	−27.03	1	30.45	H
ATOM	3681	HG1	THR B	205	6.087	33.3	−26.103	1	34.52	H
ATOM	3682	HG21	THR B	205	4.286	33.174	−28.305	1	29.92	H
ATOM	3683	HG22	THR B	205	2.981	32.784	−27.506	1	29.92	H
ATOM	3684	HG23	THR B	205	3.897	33.964	−26.994	1	29.92	H
ATOM	3685	N	PRO B	206	1.645	31.917	−24.977	1	18	N
ATOM	3686	CA	PRO B	206	0.35	31.248	−25.14	1	17.87	C
ATOM	3687	C	PRO B	206	0.05	30.892	−26.593	1	20.2	C
ATOM	3688	O	PRO B	206	0.187	31.737	−27.477	1	14.53	O
ATOM	3689	CB	PRO B	206	−0.655	32.286	−24.621	1	22.87	C
ATOM	3690	CG	PRO B	206	0.134	33.198	−23.763	1	22.22	C
ATOM	3691	CD	PRO B	206	1.494	33.257	−24.382	1	21.86	C
ATOM	3692	HA	PRO B	206	0.306	30.45	−24.591	1	21.45	H
ATOM	3693	HB2	PRO B	206	−1.042	32.767	−25.369	1	27.45	H
ATOM	3694	HB3	PRO B	206	−1.345	31.841	−24.104	1	27.45	H
ATOM	3695	HG2	PRO B	206	−0.277	34.077	−23.758	1	26.66	H
ATOM	3696	HG3	PRO B	206	0.183	32.839	−22.864	1	26.66	H
ATOM	3697	HD2	PRO B	206	1.525	33.939	−25.071	1	26.23	H
ATOM	3698	HD3	PRO B	206	2.171	33.404	−23.703	1	26.23	H
ATOM	3699	N	ASN B	207	−0.342	29.644	−26.829	1	19.17	N
ATOM	3700	CA	ASN B	207	−0.792	29.207	−28.146	1	16.49	C
ATOM	3701	C	ASN B	207	−1.897	28.165	−28.01	1	19.54	C
ATOM	3702	0	ASN B	207	−2.061	27.557	−26.95	1	15.66	O
ATOM	3703	CB	ASN B	207	0.371	28.628	−28.961	1	19.53	C
ATOM	3704	CG	ASN B	207	1.225	29.702	−29.62	1	16.92	C
ATOM	3705	OD1	ASN B	207	0.877	30.221	−30.681	1	16.98	O
ATOM	3706	ND2	ASN B	207	2.356	30.023	−29.002	1	17.66	N
ATOM	3707	H	ASN B	207	−0.356	29.022	−26.235	1	23	H
ATOM	3708	HA	ASN B	207	−1.151	29.968	−28.629	1	19.79	H
ATOM	3709	HB2	ASN B	207	0.943	28.111	−28.372	1	23.43	H
ATOM	3710	HB3	ASN B	207	0.014	28.058	−29.66	1	23.43	H
ATOM	3711	HD21	ASN B	207	2.872	30.625	−29.336	1	21.19	H
ATOM	3712	HD22	ASN B	207	2.572	29.63	−28.268	1	21.19	H
ATOM	3713	N	THR B	208	−2.662	27.961	−29.077	1	16.41	N
ATOM	3714	CA	THR B	208	−3.612	26.859	−29.105	1	14.55	C
ATOM	3715	C	THR B	208	−2.801	25.564	−29.139	1	16.01	C
ATOM	3716	O	THR B	208	−1.589	25.596	−29.359	1	12.88	O
ATOM	3717	CB	THR B	208	−4.568	26.951	−30.307	1	14.56	C
ATOM	3718	OG1	THR B	208	−3.821	27.017	−31.528	1	15.04	O
ATOM	3719	CG2	THR B	208	−5.45	28.186	−30.187	1	15.59	C
ATOM	3720	H	THR B	208	−2.65	28.442	−29.79	1	19.7	H
ATOM	3721	HA	THR B	208	−4.14	26.868	−28.292	1	17.46	H
ATOM	3722	HB	THR B	208	−5.141	26.168	−30.322	1	17.48	H
ATOM	3723	HG1	THR B	208	−4.345	27.067	−32.183	1	18.05	H
ATOM	3724	HG21	THR B	208	−6.051	28.239	−30.947	1	18.71	H
ATOM	3725	HG22	THR B	208	−5.975	28.14	−29.372	1	18.71	H
ATOM	3726	HG23	THR B	208	−4.9	28.984	−30.164	1	18.71	H
ATOM	3727	N	TYR B	209	−3.446	24.429	−28.895	1	13.5	N
ATOM	3728	CA	TYR B	209	−2.703	23.175	−28.8	1	13	C
ATOM	3729	C	TYR B	209	−3.513	21.958	−29.226	1	14.49	C
ATOM	3730	O	TYR B	209	−4.744	21.996	−29.295	1	11.51	O
ATOM	3731	CB	TYR B	209	−2.187	22.983	−27.371	1	14	C
ATOM	3732	CG	TYR B	209	−3.26	22.967	−26.303	1	13.42	C
ATOM	3733	CD1	TYR B	209	−3.864	24.146	−25.876	1	15.48	C
ATOM	3734	CD2	TYR B	209	−3.65	21.777	−25.703	1	14.21	C
ATOM	3735	CE1	TYR B	209	−4.84	24.134	−24.894	1	19.28	C
ATOM	3736	CE2	TYR B	209	−4.619	21.755	−24.72	1	19.66	C
ATOM	3737	CZ	TYR B	209	−5.211	22.935	−24.319	1	20.66	C
ATOM	3738	OH	TYR B	209	−6.178	22.907	−23.343	1	19.94	O
ATOM	3739	H	TYR B	209	−4.295	24.355	−28.783	1	16.2	H
ATOM	3740	HA	TYR B	209	−1.931	23.231	−29.385	1	15.6	H
ATOM	3741	HB2	TYR B	209	−1.714	22.137	−27.325	1	16.8	H
ATOM	3742	HB3	TYR B	209	−1.577	23.708	−27.163	1	16.8	H
ATOM	3743	HD1	TYR B	209	−3.615	24.954	−26.263	1	18.58	H
ATOM	3744	HD2	TYR B	209	−3.253	20.979	−25.971	1	17.06	H
ATOM	3745	HE1	TYR B	209	−5.24	24.928	−24.621	1	23.13	H
ATOM	3746	HE2	TYR B	209	−4.874	20.949	−24.333	1	23.6	H
ATOM	3747	HH	TYR B	209	−6.458	23.684	−23.193	1	23.92	H
ATOM	3748	N	ILE B	210	−2.782	20.885	−29.516	1	14.8	N
ATOM	3749	CA	ILE B	210	−3.348	19.627	−29.975	1	18.21	C
ATOM	3750	C	ILE B	210	−3.006	18.514	−28.994	1	15.01	C
ATOM	3751	O	ILE B	210	−1.834	18.276	−28.705	1	15.25	O
ATOM	3752	CB	ILE B	210	−2.818	19.246	−31.373	1	15.54	C
ATOM	3753	CG1	ILE B	210	−3.11	20.366	−32.375	1	15.83	C
ATOM	3754	CG2	ILE B	210	−3.438	17.936	−31.837	1	14.28	C
ATOM	3755	CD1	ILE B	210	−2.421	20.193	−33.707	1	18.37	C
ATOM	3756	H	ILE B	210	−1.924	20.865	−29.452	1	17.76	H
ATOM	3757	HA	ILE B	210	−4.314	19.706	−30.024	1	21.85	H
ATOM	3758	HB	ILE B	210	−1.857	19.127	−31.315	1	18.65	H
ATOM	3759	HG12	ILE B	210	−4.066	20.397	−32.538	1	18.99	H
ATOM	3760	HG13	ILE B	210	−2.814	21.208	−31.996	1	18.99	H
ATOM	3761	HG21	ILE B	210	−3.09	17.718	−32.716	1	17.13	H
ATOM	3762	HG22	ILE B	210	−3.207	17.237	−31.207	1	17.13	H
ATOM	3763	HG23	ILE B	210	−4.401	18.041	−31.879	1	17.13	H
ATOM	3764	HD11	ILE B	210	−2.655	20.938	−34.282	1	22.04	H
ATOM	3765	HD12	ILE B	210	−1.461	20.172	−33.565	1	22.04	H
ATOM	3766	HD13	ILE B	210	−2.714	19.36	−34.108	1	22.04	H
ATOM	3767	N	CYS B	211	−4.031	17.845	−28.478	1	13.03	N
ATOM	3768	CA	CYS B	211	−3.838	16.677	−27.628	1	16.24	C
ATOM	3769	C	CYS B	211	−3.968	15.42	−28.469	1	20.33	C
ATOM	3770	O	CYS B	211	−4.712	15.394	−29.452	1	17.44	O
ATOM	3771	CB	CYS B	211	−4.848	16.651	−26.479	1	22.87	C
ATOM	3772	SG	CYS B	211	−4.586	17.937	−25.24	1	32.56	S
ATOM	3773	H	CYS B	211	−4.856	18.049	−28.607	1	15.64	H
ATOM	3774	HA	CYS B	211	−2.945	16.699	−27.249	1	19.49	H
ATOM	3775	HB2	CYS B	211	−5.739	16.77	−26.844	1	27.44	H
ATOM	3776	HB3	CYS B	211	−4.789	15.793	−26.031	1	27.44	H
ATOM	3777	N	MET B	212	−3.236	14.385	−28.075	1	20.62	N
ATOM	3778	CA	MET B	212	−3.224	13.123	−28.796	1	19.04	C
ATOM	3779	C	MET B	212	−3.266	11.958	−27.822	1	24.41	C
ATOM	3780	0	MET B	212	−2.621	11.994	−26.773	1	20.8	O
ATOM	3781	CB	MET B	212	−1.982	13.025	−29.676	1	22.84	C
ATOM	3782	CG	MET B	212	−1.792	11.672	−30.333	1	22.92	C
ATOM	3783	SD	MET B	212	−0.403	11.689	−31.475	1	24.54	S
ATOM	3784	CE	MET B	212	−0.348	9.97	−31.974	1	31.53	C
ATOM	3785	H	MET B	212	−2.729	14.391	−27.38	1	24.74	H
ATOM	3786	HA	MET B	212	−4.003	13.081	−29.372	1	22.85	H
ATOM	3787	HB2	MET B	212	−2.047	13.688	−30.381	1	27.41	H
ATOM	3788	HB3	MET B	212	−1.199	13.201	−29.131	1	27.41	H
ATOM	3789	HG2	MET B	212	−1.616	11.006	−29.65	1	27.5	H
ATOM	3790	HG3	MET B	212	−2.592	11.441	−30.83	1	27.5	H
ATOM	3791	HE1	MET B	212	0.378	9.849	−32.605	1	37.83	H
ATOM	3792	HE2	MET B	212	−0.2	9.419	−31.189	1	37.83	H
ATOM	3793	HE3	MET B	212	−1.192	9.735	−32.39	1	37.83	H
ATOM	3794	N	GLN B	213	−4.031	10.931	−28.178	1	22.35	N
ATOM	3795	CA	GLN B	213	−4.116	9.713	−27.386	1	24.56	C
ATOM	3796	C	GLN B	213	4.148	8.501	−28.309	1	31.59	C
ATOM	3797	O	GLN B	213	−5.071	8.346	−29.111	1	28.14	O
ATOM	3798	CB	GLN B	213	−5.357	9.735	−26.493	1	27.78	C
ATOM	3799	CG	GLN B	213	−5.48	8.534	−25.565	1	30.43	C
ATOM	3800	CD	GLN B	213	−6.836	8.462	−24.893	1	33.92	C
ATOM	3801	OE1	GLN B	213	−7.736	7.766	−25.363	1	34.06	O
ATOM	3802	NE2	GLN B	213	−6.991	9.185	−23.788	1	30.76	N
ATOM	3803	H	GLN B	213	−4.519	10.917	−28.886	1	26.82	H
ATOM	3804	HA	GLN B	213	−3.333	9.644	−26.818	1	29.47	H
ATOM	3805	HB2	GLN B	213	−5.329	10.533	−25.941	1	33.34	H
ATOM	3806	HB3	GLN B	213	−6.145	9.755	−27.057	1	33.34	H
ATOM	3807	HG2	GLN B	213	−5.356	7.722	−26.08	1	36.51	H
ATOM	3808	HG3	GLN B	213	−4.803	8.597	−24.873	1	36.51	H
ATOM	3809	HE21	GLN B	213	−7.742	9.177	−23.371	1	36.91	H
ATOM	3810	HE22	GLN B	213	−6.339	9.661	−23.491	1	36.91	H
ATOM	3811	N	ARG B	214	−3.137	7.645	−28.192	1	26.52	N
ATOM	3812	CA	ARG B	214	−3.047	6.45	−29.023	1	33.12	C
ATOM	3813	C	ARG B	214	−4.103	5.415	−28.633	1	37.91	C
ATOM	3814	O	ARG B	214	−4.624	5.431	−27.514	1	34.52	O
ATOM	3815	CB	ARG B	214	−1.646	5.838	−28.929	1	42.25	C
ATOM	3816	CG	ARG B	214	−0.556	6.668	−29.617	1	42.31	C
ATOM	3817	CD	ARG B	214	0.652	5.824	−30.026	1	42.8	C
ATOM	3818	NE	ARG B	214	0.268	4.633	−30.787	1	51.67	N
ATOM	3819	CZ	ARG B	214	0.147	4.575	−32.112	1	45.75	C
ATOM	3820	NH1	ARG B	214	0.385	5.64	−32.865	1	40.29	N
ATOM	3821	NH2	ARG B	214	−0.212	3.438	−32.692	1	44.7	N
ATOM	3822	H	ARG B	214	−2.488	7.735	−27.635	1	31.82	H
ATOM	3823	HA	ARG B	214	−3.201	6.699	−29.947	1	39.74	H
ATOM	3824	HB2	ARG B	214	−1.405	5.751	−27.993	1	50.7	H
ATOM	3825	HB3	ARG B	214	−1.659	4.963	−29.347	1	50.7	H
ATOM	3826	HG2	ARG B	214	−0.924	7.074	−30.417	1	50.77	H
ATOM	3827	HG3	ARG B	214	−0.248	7.356	−29.006	1	50.77	H
ATOM	3828	HD2	ARG B	214	1.24	6.36	−30.582	1	51.36	H
ATOM	3829	HD3	ARG B	214	1.122	5.534	−29.228	1	51.36	H
ATOM	3830	HE	ARG B	214	0.108	3.914	−30.343	1	62	H
ATOM	3831	HH11	ARG B	214	0.617	6.382	−32.498	1	48.35	H
ATOM	3832	HH12	ARG B	214	0.304	5.589	−33.719	1	48.35	H
ATOM	3833	HH21	ARG B	214	−0.367	2.741	−32.213	1	53.64	H
ATOM	3834	HH22	ARG B	214	−0.289	3.397	−33.548	1	53.64	H
ATOM	3835	N	THR B	215	−4.411	4.526	−29.575	1	42.55	N
ATOM	3836	CA	THR B	215	−5.441	3.504	−29.396	1	47.95	C
ATOM	3837	C	THR B	215	−6.789	4.141	−29.072	1	47.59	C
ATOM	3838	O	THR B	215	−7.69	4.169	−29.914	1	48.2	O
ATOM	3839	CB	THR B	215	−5.061	2.502	−28.283	1	45.58	C
ATOM	3840	OG1	THR B	215	−3.858	1.816	−28.651	1	50.86	O
ATOM	3841	CG2	THR B	215	−6.166	1.475	−28.071	1	55.86	C
ATOM	3842	H	THR B	215	−4.028	4.494	−30.344	1	51.06	H
ATOM	3843	HA	THR B	215	−5.537	3.008	−30.223	1	57.54	H
ATOM	3844	HB	THR B	215	−4.92	2.98	−27.451	1	54.7	H
ATOM	3845	HG1	THR B	215	−3.645	1.269	−28.05	1	61.03	H
ATOM	3846	HG21	THR B	215	−5.911	0.855	−27.37	1	67.03	H
ATOM	3847	HG22	THR B	215	−6.988	1.922	−27.814	1	67.03	H
ATOM	3848	HG23	THR B	215	−6.32	0.98	−28.891	1	67.03	H
TER	3849		THR B	215
ATOM	3850	N	GLU C	93	−21.096	71.394	−8.126	1	57.72	N
ATOM	3851	CA	GLU C	93	−19.991	72.179	−7.586	1	64.4	C
ATOM	3852	C	GLU C	93	−18.719	71.951	−8.396	1	60.46	C
ATOM	3853	O	GLU C	93	−18.309	72.806	−9.183	1	62.51	O
ATOM	3854	CB	GLU C	93	−19.747	71.824	−6.115	1	58.36	C
ATOM	3855	CG	GLU C	93	−18.795	72.76	−5.383	1	58.1	C
ATOM	3856	CD	GLU C	93	−19.458	74.063	−4.971	1	61.87	C
ATOM	3857	OE1	GLU C	93	−20.558	74.362	−5.481	1	60.81	O
ATOM	3858	OE2	GLU C	93	−18.885	74.786	−4.129	1	60.23	O1−
ATOM	3859	HA	GLU C	93	−20.216	73.122	−7.636	1	77.28	H
ATOM	3860	HB2	GLU C	93	−20.596	71.844	−5.647	1	70.03	H
ATOM	3861	HB3	GLU C	93	−19.371	70.93	−6.071	1	70.03	H
ATOM	3862	HG2	GLU C	93	−18.474	72.32	−4.58	1	69.72	H
ATOM	3863	HG3	GLU C	93	−18.05	72.973	−5.966	1	69.72	H
ATOM	3864	N	SER C	94	−18.107	70.787	−8.197	1	55.28	N
ATOM	3865	CA	SER C	94	−16.857	70.437	−8.856	1	48.47	C
ATOM	3866	C	SER C	94	−16.938	69.038	−9.447	1	42.81	C
ATOM	3867	O	SER C	94	−17.428	68.105	−8.805	1	35	O
ATOM	3868	CB	SER C	94	−15.69	70.525	−7.872	1	51.57	C
ATOM	3869	OG	SER C	94	−15.518	71.852	−7.409	1	59.31	O
ATOM	3870	H	SER C	94	−18.404	70.172	−7.673	1	66.34	H
ATOM	3871	HA	SER C	94	−16.691	71.062	−9.579	1	58.16	H
ATOM	3872	HB2	SER C	94	−15.872	69.947	−7.115	1	61.88	H
ATOM	3873	HB3	SER C	94	−14.878	70.239	−8.32	1	61.88	H
ATOM	3874	HG	SER C	94	−14.875	71.887	−6.87	1	71.18	H
ATOM	3875	N	TYR C	95	−16.457	68.908	−10.678	1	41.19	N
ATOM	3876	CA	TYR C	95	−16.444	67.634	−11.379	1	38.72	C
ATOM	3877	C	TYR C	95	−15.019	67.168	−11.629	1	38.41	C
ATOM	3878	O	TYR C	95	−14.099	67.975	−11.764	1	32.89	O
ATOM	3879	CB	TYR C	95	−17.19	67.743	−12.708	1	37.08	C
ATOM	3880	CG	TYR C	95	−18.693	67.809	−12.573	1	37.6	C
ATOM	3881	CD1	TYR C	95	−19.338	69.017	−12.344	1	41.89	C
ATOM	3882	CD2	TYR C	95	−19.469	66.663	−12.685	1	34.68	C
ATOM	3883	CE1	TYR C	95	−20.712	69.08	−12.226	1	39.87	C
ATOM	3884	CE2	TYR C	95	−20.842	66.716	−12.569	1	36.52	C
ATOM	3885	CZ	TYR C	95	−21.459	67.926	−12.34	1	40.73	C
ATOM	3886	OH	TYR C	95	−22.829	67.98	−12.225	1	41.72	O
ATOM	3887	H	TYR C	95	−16.127	69.557	−11.136	1	49.43	H
ATOM	3888	HA	TYR C	95	−16.89	66.966	−10.835	1	46.47	H
ATOM	3889	HB2	TYR C	95	−16.899	68.549	−13.162	1	44.49	H
ATOM	3890	HB3	TYR C	95	−16.976	66.967	−13.249	1	44.49	H
ATOM	3891	HD1	TYR C	95	−18.837	69.797	−12.267	1	50.27	H
ATOM	3892	HD2	TYR C	95	−19.055	65.845	−12.84	1	41.62	H
ATOM	3893	HE1	TYR C	95	−21.132	69.895	−12.072	1	47.85	H
ATOM	3894	HE2	TYR C	95	−21.348	65.94	−12.645	1	43.82	H
ATOM	3895	HH	TYR C	95	−23.074	68.771	−12.087	1	50.06	H
ATOM	3896	N	CYS C	96	−14.853	65.853	−11.684	1	35.27	N
ATOM	3897	CA	CYS C	96	−13.59	65.246	−12.064	1	33.31	C
ATOM	3898	C	CYS C	96	−13.632	64.911	−13.55	1	27.94	C
ATOM	3899	O	CYS C	96	−14.616	64.36	−14.036	1	24.96	O
ATOM	3900	CB	CYS C	96	−13.329	63.99	−11.232	1	32.47	C
ATOM	3901	SG	CYS C	96	−11.682	63.299	−11.433	1	36.22	S
ATOM	3902	H	CYS C	96	−15.47	65.283	−11.503	1	42.33	H
ATOM	3903	HA	CYS C	96	−12.867	65.874	−11.909	1	39.98	H
ATOM	3904	HB2	CYS C	96	−13.445	64.208	−10.294	1	38.96	H
ATOM	3905	HB3	CYS C	96	−13.969	63.307	−11.49	1	38.96	H
ATOM	3906	N	GLY C	97	−12.573	65.259	−14.272	1	28.67	N
ATOM	3907	CA	GLY C	97	−12.49	64.946	−15.687	1	31.01	C
ATOM	3908	C	GLY C	97	−12.065	66.13	−16.535	1	33.85	C
ATOM	3909	O	GLY C	97	−11.45	67.067	−16.028	1	35.84	O
ATOM	3910	H	GLY C	97	−11.888	65.677	−13.962	1	34.4	H
ATOM	3911	HA2	GLY C	97	−11.849	64.23	−15.82	1	37.22	H
ATOM	3912	HA3	GLY C	97	−13.357	64.643	−16	1	37.22	H
ATOM	3913	N	PRO C	98	−12.391	66.097	−17.837	1	33.61	N
ATOM	3914	CA	PRO C	98	−13.165	65.036	−18.492	1	34.25	C
ATOM	3915	C	PRO C	98	−12.428	63.695	−18.552	1	32.91	C
ATOM	3916	O	PRO C	98	−11.2	63.661	−18.522	1	33.58	O
ATOM	3917	CB	PRO C	98	−13.4	65.596	−19.897	1	43.48	C
ATOM	3918	CG	PRO C	98	−12.285	66.542	−20.119	1	44.16	C
ATOM	3919	CD	PRO C	98	−11.991	67.149	−18.785	1	39.32	C
ATOM	3920	HA	PRO C	98	−14.019	64.916	−18.046	1	41.1	H
ATOM	3921	HB2	PRO C	98	−13.374	64.875	−20.546	1	52.18	H
ATOM	3922	HB3	PRO C	98	−14.253	66.056	−19.928	1	52.18	H
ATOM	3923	HG2	PRO C	98	−11.512	66.06	−20.452	1	52.99	H
ATOM	3924	HG3	PRO C	98	−12.56	67.225	−20.751	1	52.99	H
ATOM	3925	HD2	PRO C	98	−11.043	67.337	−18.701	1	47.19	H
ATOM	3926	HD3	PRO C	98	−12.526	67.946	−18.651	1	47.19	H
ATOM	3927	N	CYS C	99	−13.195	62.61	−18.619	1	29.92	N
ATOM	3928	CA	CYS C	99	−12.656	61.259	−18.747	1	30.84	C
ATOM	3929	C	CYS C	9	−13.492	60.459	−19.732	1	33.78	C
ATOM	3930	O	CYS C	99	−14.602	60.863	−20.076	1	29.2	O
ATOM	3931	CB	CYS C	99	−12.646	60.535	−17.4	1	24.67	C
ATOM	3932	SG	CYS C	99	−11.422	61.121	−16.229	1	27.04	S
ATOM	3933	OH	CYS C	99	−14.054	62.632	−18.593	1	35.9	H
ATOM	3934	HA	CYS C	99	−11.746	61.303	−19.079	1	37.01	H
ATOM	3935	HB2	CYS C	99	−13.518	60.639	−16.987	1	29.6	H
ATOM	3936	HB3	CYS C	99	−12.473	59.593	−17.557	1	29.6	H
ATOM	3937	N	PRO C	100	−12.963	59.314	−20.19	1	30.07	N
ATOM	3938	CA	PRO C	100	−13.8	58.399	−20.968	1	29.87	C
ATOM	3939	C	PRO C	100	−14.997	57.928	−20.148	1	33.56	C
ATOM	3940	O	PRO C	100	−14.919	57.895	−18.917	1	26.53	O
ATOM	3941	CB	PRO C	100	−12.852	57.239	−21.291	1	30.74	C
ATOM	3942	CG	PRO C	100	−11.483	57.83	−21.199	1	29.98	C
ATOM	3943	CD	PRO C	100	−11.566	58.853	−20.11	1	28.76	C
ATOM	3944	HA	PRO C	100	−14.102	58.818	−21.789	1	35.84	H
ATOM	3945	HB2	PRO C	100	−12.965	56.531	−20.638	1	36.89	H
ATOM	3946	HB3	PRO C	100	−13.026	56.912	−22.188	1	36.89	H
ATOM	3947	HG2	PRO C	100	−10.843	57.138	−20.971	1	35.98	H
ATOM	3948	HG3	PRO C	100	−11.251	58.248	−22.043	1	35.98	H
ATOM	3949	HD2	PRO C	100	−11.393	58.444	−19.247	1	34.51	H
ATOM	3950	HD3	PRO C	100	−10.956	59.586	−20.286	1	34.51	H
ATOM	3951	N	LYS C	101	−16.086	57.579	−20.825	1	31.45	N
ATOM	3952	CA	LYS C	101	−17.315	57.171	−20.154	1	38.12	C
ATOM	3953	C	LYS C	101	−17.066	56.015	−19.182	1	30.89	C
ATOM	3954	O	LYS C	101	−16.41	55.034	−19.529	1	28.71	O
ATOM	3955	CB	LYS C	101	−18.373	56.768	−21.188	1	43.7	C
ATOM	3956	CG	LYS C	101	−19.776	56.557	−20.62	1	55.1	C
ATOM	3957	CD	LYS C	101	−20.514	57.877	−20.423	1	71.07	C
ATOM	3958	CE	LYS C	101	−21.918	57.662	−19.866	1	83.53	C
ATOM	3959	NZ	LYS C	101	−22.935	57.438	−20.932	1	96.55	N1+
ATOM	3960	H	LYS C		101	−16.139	57.57	−21.684	1	37.74	H
ATOM	3961	HA	LYS C	101	−17.662	57.921	−19.645	1	45.75	H
ATOM	3962	HB2	LYS C	101	−18.431	57.465	−21.86	1	52.44	H
ATOM	3963	HB3	LYS C	101	−18.098	55.936	−21.605	1	52.44	H
ATOM	3964	HG2	LYS C	101	−20.291	56.011	−21.235	1	66.13	H
ATOM	3965	HG3	LYS C		101	−19.708	56.117	−19.758	1	66.13	H
ATOM	3966	HD2	LYS C	101	−20.02	58.428	−19.797	1	85.28	H
ATOM	3967	HD3	LYS C	101	−20.593	58.329	−21.278	1	85.28	H
ATOM	3968	HE2	LYS C	101	−21.912	56.882	−19.288	1	100.24	H
ATOM	3969	HE3	LYS C	101	−22.18	58.447	−19.36	1	100.24	H
ATOM	3970	HZ1	LYS C	101	−23.738	57.318	−20.567	1	115.86	H
ATOM	3971	HZ2	LYS C	101	−22.967	58.143	−21.474	1	115.86	H
ATOM	3972	HZ3	LYS C	101	−22.723	56.717	−21.409	1	115.86	H
ATOM	3973	N	ASN C	102	−17.578	56.16	−17.962	1	29.4	N
ATOM	3974	CA	ASN C	102	−17.566	55.095	−16.957	1	21.26	C
ATOM	3975	C	ASN C	102	−16.171	54.67	−16.501	1	23.13	C
ATOM	3976	O	ASN C	102	−15.98	53.538	−16.052	1	23.84	O
ATOM	3977	CB	ASN C	102	−18.317	53.871	−17.484	1	26.84	C
ATOM	3978	CG	ASN C	102	−19.758	54.178	−17.827	1	37.5	C
ATOM	3979	OD1	ASN C	102	−20.39	55.027	−17.198	1	35.99	O
ATOM	3980	ND2	ASN C	102	−20.288	53.491	−18.833	1	39.34	N
ATOM	3981	H	ASN C	102	−17.948	56.885	−17.684	1	35.28	H
ATOM	3982	HA	ASN C	102	−18.042	55.411	−16.173	1	25.51	H
ATOM	3983	HB2	ASN C	102	−17.878	53.551	−18.287	1	32.21	H
ATOM	3984	HB3	ASN C	102	−18.311	53.179	−16.804	1	32.21	H
ATOM	3985	HD21	ASN C	102	−21.104	53.63	−19.066	1	47.21	H
ATOM	3986	HD22	ASN C	102	−19.814	52.907	−19.251	1	47.21	H
ATOM	3987	N	TRP C	103	−15.202	55.573	−16.611	1	20.5	N
ATOM	3988	CA	TRP C	103	−13.88	55.343	−16.034	1	23.43	C
ATOM	3989	C	TRP C	103	−13.826	55.907	−14.62	1	21.27	C
ATOM	3990	O	TRP C	103	−14.659	56.727	−14.239	1	23.07	O
ATOM	3991	CB	TRP C	103	−12.785	55.984	−16.889	1	21.36	C
ATOM	3992	CG	TRP C	103	−12.438	55.213	−18.124	1	22.71	C
ATOM	3993	CD1	TRP C	103	−13.27	54.42	−18.857	1	24.15	C
ATOM	3994	CD2	TRP C	103	−11.158	55.158	−18.771	1	19.27	C
ATOM	3995	NE1	TRP C	103	−12.591	53.88	−19.923	1	20.72	N
ATOM	3996	CE2	TRP C	103	−11.293	54.317	−19.891	1	20.3	C
ATOM	3997	CE3	TRP C	103	−9.914	55.737	−18.508	1	20.4	C
ATOM	3998	CZ2	TRP C	103	−10.23	54.042	−20.751	1	24.78	C
ATOM	3999	CZ3	TRP C	103	−8.862	55.465	−19.36	1	20.79	C
ATOM	4000	CH2	TRP C	103	−9.026	54.624	−20.468	1	22.99	C
ATOM	4001	H	TRP C	103	−15.284	56.328	−17.014	1	24.6	H
ATOM	4002	HA	TRP C	103	−13.712	54.389	−15.989	1	28.12	H
ATOM	4003	HB2	TRP C	103	−13.082	56.865	−17.165	1	25.64	H
ATOM	4004	HB3	TRP C	103	−11.979	56.063	−16.355	1	25.64	H
ATOM	4005	HD1	TRP C	103	−14.169	54.273	−18.669	1	28.98	H
ATOM	4006	HE1	TRP C	103	−12.926	53.352	−20.514	1	24.87	H
ATOM	4007	HE3	TRP C	103	−9.797	56.298	−17.776	1	24.47	H
ATOM	4008	HZ2	TRP C	103	−10.336	53.482	−21.486	1	29.74	H
ATOM	4009	HZ3	TRP C	103	−8.03	55.848	−19.196	1	24.95	H
ATOM	4010	HH2	TRP C	103	−8.299	54.458	−21.025	1	27.58	H
ATOM	4011	N	ILE C	104	−12.852	55.455	−13.838	1	21.47	N
ATOM	4012	CA	ILE C	104	−12.562	56.076	−12.552	1	22.27	C
ATOM	4013	C	ILE C	104	−11.92	57.428	−12.799	1	20.16	C
ATOM	4014	O	ILE C	104	−11.097	57.559	−13.694	1	20.4	O
ATOM	4015	CB	ILE C	104	−11.618	55.218	−11.691	1	20.98	C
ATOM	4016	CG1	ILE C	104	−12.318	53.922	−11.276	1	23.82	C
ATOM	4017	CG2	ILE C	104	−11.151	56.005	−10.452	1	22.89	C
ATOM	4018	CD1	ILE C	104	−11.469	53	−10.418	1	32.17	C
ATOM	4019	H	ILE C	104	−12.343	54.789	−14.03	1	25.76	H
ATOM	4020	HA	ILE C	104	−13.389	56.212	−12.062	1	26.72	H
ATOM	4021	HB	ILE C	104	−10.839	54.991	−12.222	1	25.18	H
ATOM	4022	HG12	ILE C	104	−13.114	54.147	−10.769	1	28.58	H
ATOM	4023	HG13	ILE C	104	−12.567	53.433	−12.076	1	28.58	H
ATOM	4024	HG21	ILE C	104	−10.559	55.444	−9.927	1	27.46	H
ATOM	4025	HG22	ILE C	104	−10.681	56.802	−10.744	1	27.46	H
ATOM	4026	HG23	ILE C	104	−11.927	56.252	−9.925	1	27.46	H
ATOM	4027	HD11	ILE C	104	−11.984	52.208	−10.201	1	38.61	H
ATOM	4028	HD12	ILE C	104	−10.673	52.752	−10.915	1	38.61	H
ATOM	4029	HD13	ILE C	104	−11.22	53.467	−9.605	1	38.61	H
ATOM	4030	N	CYS C	105	−12.291	58.426	−12.005	1	18.5	N
ATOM	4031	CA	CYS C	105	−11.642	59.73	−12.068	1	21.47	C
ATOM	4032	C	CYS C	105	−11.168	60.124	−10.673	1	24.11	C
ATOM	4033	O	CYS C	105	−11.949	60.137	−9.72	1	22.75	O
ATOM	4034	CB	CYS C	105	−12.592	60.783	−12.641	1	24.61	C
ATOM	4035	SG	CYS C	105	−11.757	62.29	−13.195	1	30.83	S
ATOM	4036	H	CYS C	105	−12.918	58.373	−11.418	1	22.2	H
ATOM	4037	HA	CYS C	105	−10.867	59.673	−12.648	1	25.76	H
ATOM	4038	HB2	CYS C	105	−13.056	60.403	−13.404	1	29.53	H
ATOM	4039	HB3	CYS C	105	−13.232	61.032	−11.957	1	29.53	H
ATOM	4040	N	TYR C	106	−9.88	60.43	−10.556	1	20.57	N
ATOM	4041	CA	TYR C	106	−9.279	60.704	−9.259	1	19.53	C
ATOM	4042	C	TYR C	106	−8.063	61.607	−9.395	1	24.23	C
ATOM	4043	O	TYR C	106	−7.074	61.243	−10.036	1	18.6	O
ATOM	4044	CB	TYR C	106	−8.885	59.394	−8.58	1	18.96	C
ATOM	4045	CG	TYR C	106	−8.336	59.537	−7.183	1	17.51	C
ATOM	4046	CD1	TYR C	106	−9.161	59.887	−6.128	1	20.97	C
ATOM	4047	CD2	TYR C	106	−6.995	59.293	−6.912	1	20.26	C
ATOM	4048	CE1	TYR C	106	−8.669	60.006	−4.846	1	22.2	C
ATOM	4049	CE2	TYR C	106	−6.494	59.405	−5.629	1	20.01	C
ATOM	4050	CZ	TYR C	106	−7.339	59.764	−4.599	1	22.79	C
ATOM	4051	OH	TYR C	106	−6.864	59.881	−3.313	1	24.09	O
ATOM	4052	H	TYR C	106	−9.332	60.486	−11.217	1	24.68	H
ATOM	4053	HA	TYR C	106	−9.928	61.153	−8.696	1	23.44	H
ATOM	4054	HB2	TYR C	106	−9.67	58.826	−8.529	1	22.75	H
ATOM	4055	HB3	TYR C	106	−8.205	58.96	−9.119	1	22.75	H
ATOM	4056	HD1	TYR C	106	−10.062	60.051	−6.288	1	25.17	H
ATOM	4057	HD2	TYR C	106	−6.425	59.049	−7.606	1	24.31	H
ATOM	4058	HE1	TYR C	106	−9.237	60.246	−4.149	1	26.64	H
ATOM	4059	HE2	TYR C	106	−5.594	59.243	−5.461	1	24.02	H
ATOM	4060	HH	TYR C	106	−6.042	59.709	−3.293	1	28.9	H
ATOM	4061	N	LYS C	107	−8.157	62.784	−8.783	1	23.77	N
ATOM	4062	CA	LYS C	107	−7.07	63.754	−8.756	1	22.66	C
ATOM	4063	C	LYS C	107	−6.482	63.992	−10.144	1	26.25	C
ATOM	4064	O	LYS C	107	−5.304	63.722	−10.384	1	25.69	O
ATOM	4065	CB	LYS C	107	−5.982	63.288	−7.786	1	23.7	C
ATOM	4066	CG	LYS C	107	−6.453	63.225	−6.341	1	25.76	C
ATOM	4067	CD	LYS C	107	−5.337	62.83	−5.392	1	24.07	C
ATOM	4068	CE	LYS C	107	−5.787	62.932	−3.946	1	25.09	C
ATOM	4069	NZ	LYS C	107	−4.764	62.412	−3.002	1	28.21	N1+
ATOM	4070	H	LYS C	107	−8.86	63.049	−8.365	1	28.53	H
ATOM	4071	HA	LYS C	107	−7.415	64.6	−8.431	1	27.19	H
ATOM	4072	HB2	LYS C	107	−5.69	62.399	−8.043	1	28.45	H
ATOM	4073	HB3	LYS C	107	−5.236	63.906	−7.83	1	28.45	H
ATOM	4074	HG2	LYS C	107	−6.78	64.099	−6.076	1	30.91	H
ATOM	4075	HG3	LYS C	107	−7.161	62.567	−6.266	1	30.91	H
ATOM	4076	HD2	LYS C	107	−5.077	61.911	−5.566	1	28.88	H
ATOM	4077	HD3	LYS C	107	−4.581	63.424	−5.519	1	28.88	H
ATOM	4078	HE2	LYS C	107	−5.952	63.863	−3.729	1	30.11	H
ATOM	4079	HE3	LYS C	107	−6.599	62.414	−3.828	1	30.11	H
ATOM	4080	HZ1	LYS C	107	−4.009	62.875	−3.086	1	33.85	H
ATOM	4081	HZ2	LYS C	107	−5.058	62.486	−2.165	1	33.85	H
ATOM	4082	HZ3	LYS C	107	−4.598	61.555	−3.175	1	33.85	H
ATOM	4083	N	ASN C	108	−7.324	64.477	−11.052	1	24.3	N
ATOM	4084	CA	ASN C	108	−6.908	64.862	−12.399	1	29.43	C
ATOM	4085	C	ASN C	108	−6.39	63.7	−13.248	1	29.94	C
ATOM	4086	O	ASN C	108	−5.692	63.92	−14.238	1	30.74	O
ATOM	4087	CB	ASN C	108	−5.834	65.95	−12.322	1	37.42	C
ATOM	4088	CG	ASN C	108	−6.243	67.111	−11.434	1	39.33	C
ATOM	4089	OD1	ASN C	108	−7.357	67.623	−11.536	1	36.77	O
ATOM	4090	ND2	ASN C	108	−5.341	67.526	−10.549	1	38.25	N
ATOM	4091	H	ASN C	108	−8.163	64.595	−10.908	1	29.16	H
ATOM	4092	HA	ASN C	108	−7.674	65.239	−12.859	1	35.31	H
ATOM	4093	HB2	ASN C	108	−5.02	65.566	−11.959	1	44.91	H
ATOM	4094	HB3	ASN C	108	−5.67	66.296	−13.213	1	44.91	H
ATOM	4095	HD21	ASN C	108	−5.525	68.181	−10.023	1	45.91	H
ATOM	4096	HD22	ASN C	108	−4.574	67.14	−10.503	1	45.91	H
ATOM	4097	N	ASN C	109	−6.729	62.472	−12.863	1	22.35	N
ATOM	4098	CA	ASN C	109	−6.364	61.294	−13.65	1	21.33	C
ATOM	4099	C	ASN C	109	−7.542	60.352	−13.846	1	21.79	C
ATOM	4100	O	ASN C	109	−8.331	60.125	−12.924	1	20.85	O
ATOM	4101	CB	ASN C	109	−5.211	60.538	−12.986	1	24.32	C
ATOM	4102	CG	ASN C	109	−3.921	61.337	−12.968	1	22.95	C
ATOM	4103	OD1	ASN C	109	−3.364	61.656	−14.015	1	30.85	O
ATOM	4104	ND2	ASN C	109	−3.434	61.653	−11.775	1	23.23	N
ATOM	4105	H	ASN C	109	−7.173	62.292	−12.148	1	26.82	H
ATOM	4106	HA	ASN C	109	−6.065	61.583	−14.526	1	25.6	H
ATOM	4107	HB2	ASN C	109	−5.452	60.336	−12.068	1	29.18	H
ATOM	4108	HB3	ASN C	109	−5.049	59.716	−13.475	1	29.18	H
ATOM	4109	HD21	ASN C	109	−2.705	62.105	−11.713	1	27.87	H
ATOM	4110	HD22	ASN C	109	−3.848	61.405	−11.062	1	27.87	H
ATOM	4111	N	CYS C	110	−7.646	59.804	−15.053	1	16.78	N
ATOM	4112	CA	CYS C	110	−8.675	58.825	−15.382	1	19.5	C
ATOM	4113	C	CYS C	110	−8.083	57.42	−15.392	1	18.25	C
ATOM	4114	O	CYS C	110	−6.991	57.21	−15.923	1	16.64	O
ATOM	4115	CB	CYS C	110	−9.296	59.131	−16.745	1	22.08	C
ATOM	4116	SG	CYS C	110	−9.588	60.882	−17.059	1	25.44	S
ATOM	4117	H	CYS C	110	−7.122	59.987	−15.71	1	20.14	H
ATOM	4118	HA	CYS C	110	−9.376	58.857	−14.712	1	23.4	H
ATOM	4119	HB2	CYS C	110	−8.7	58.804	−17.438	1	26.5	H
ATOM	4120	HB3	CYS C	110	−10.15	58.675	−16.807	1	26.5	H
ATOM	4121	N	TYR C	111	−8.806	56.462	−14.823	1	16.4	N
ATOM	4122	CA	TYR C	111	−8.35	55.074	−14.793	1	16.58	C
ATOM	4123	C	TYR C	111	−9.442	54.103	−15.219	1	18.92	C
ATOM	4124	O	TYR C	111	−10.626	54.362	−15.018	1	17.47	O
ATOM	4125	CB	TYR C	111	−7.872	54.69	−13.391	1	15.45	C
ATOM	4126	CG	TYR C	111	−6.797	55.583	−12.823	1	14.27	C
ATOM	4127	CD1	TYR C	111	−5.456	55.321	−13.059	1	17.54	C
ATOM	4128	CD2	TYR C	111	−7.124	56.68	−12.039	1	17.77	C
ATOM	4129	CE1	TYR C	111	−4.47	56.131	−12.535	1	19.61	C
ATOM	4130	CE2	TYR C	111	−6.148	57.495	−11.509	1	15.51	C
ATOM	4131	CZ	TYR C	111	−4.822	57.216	−11.76	1	17.01	C
ATOM	4132	OH	TYR C	111	−3.845	58.025	−11.239	1	17.34	O
ATOM	4133	H	TYR C	111	−9.569	56.589	−14.446	1	19.67	H
ATOM	4134	HA	TYR C	111	−7.603	54.973	−15.404	1	19.9	H
ATOM	4135	HB2	TYR C	111	−8.63	54.723	−12.786	1	18.53	H
ATOM	4136	HB3	TYR C	111	−7.518	53.788	−13.421	1	18.53	H
ATOM	4137	HD1	TYR C	111	−5.218	54.589	−13.58	1	21.04	H
ATOM	4138	HD2	TYR C	111	−8.019	56.868	−11.868	1	21.32	H
ATOM	4139	HE1	TYR C	111	−3.574	55.945	−12.703	1	23.53	H
ATOM	4140	HE2	TYR C	111	−6.382	58.229	−10.987	1	18.62	H
ATOM	4141	HH	TYR C	111	−4.194	58.643	−10.79	1	20.81	H
ATOM	4142	N	GLN C	112	−9.035	52.978	−15.797	1	18.21	N
ATOM	4143	CA	GLN C	112	−9.954	51.869	−16.025	1	19.09	C
ATOM	4144	C	GLN C	112	−9.246	50.536	−15.845	1	17.43	C
ATOM	4145	O	GLN C	112	−8.135	50.33	−16.337	1	15.67	O
ATOM	4146	CB	GLN C	112	−10.578	51.946	−17.416	1	21.52	C
ATOM	4147	CG	GLN C	112	−11.604	50.841	−17.706	1	22.47	C
ATOM	4148	CD	GLN C	112	−12.794	50.862	−16.753	1	23.56	C
ATOM	4149	OE1	GLN C	112	−12.685	50.483	−15.585	1	22.27	O
ATOM	4150	NE2	GLN C	112	−13.941	51.302	−17.256	1	30.82	N
ATOM	4151	H	GLN C	112	−8.231	52.831	−16.067	1	21.85	H
ATOM	4152	HA	GLN C	112	−10.671	51.917	−15.373	1	22.91	H
ATOM	4153	HB2	GLN C	112	−11.03	52.799	−17.509	1	25.83	H
ATOM	4154	HB3	GLN C	112	−9.873	51.875	−18.079	1	25.83	H
ATOM	4155	HG2	GLN C	112	−11.942	50.954	−18.608	1	26.97	H
ATOM	4156	HG3	GLN C	112	−11.17	49.978	−17.621	1	26.97	H
ATOM	4157	HE21	GLN C	112	−14.643	51.335	−16.76	1	36.99	H
ATOM	4158	HE22	GLN C	112	−13.982	51.555	−18.077	1	36.99	H
ATOM	4159	N	PHE C	113	−9.911	49.643	−15.122	1	16.74	N
ATOM	4160	CA	PHE C	113	−9.411	48.302	−14.867	1	19.52	C
ATOM	4161	C	PHE C	113	−10.086	47.323	−15.811	1	21.23	C
ATOM	4162	O	PHE C	113	−11.263	47.011	−15.651	1	24.99	O
ATOM	4163	CB	PHE C	113	−9.663	47.898	−13.415	1	17.97	C
ATOM	4164	CG	PHE C	113	−8.873	48.695	−12.419	1	25.87	C
ATOM	4165	CD1	PHE C	113	−9.189	50.019	−12.163	1	23.02	C
ATOM	4166	CD2	PHE C	113	−7.817	48.119	−11.734	1	25.71	C
ATOM	4167	CE1	PHE C	113	−8.466	50.751	−11.248	1	25.64	C
ATOM	4168	CE2	PHE C	113	−7.091	48.849	−10.815	1	27.12	C
ATOM	4169	CZ	PHE C	113	−7.416	50.166	−10.572	1	26.16	C
ATOM	4170	H	PHE C	113	−10.675	49.797	−14.759	1	20.08	H
ATOM	4171	HA	PHE C	113	−8.455	48.277	−15.031	1	23.43	H
ATOM	4172	HB2	PHE C	113	−10.604	48.022	−13.215	1	21.57	H
ATOM	4173	HB3	PHE C	113	−9.423	46.964	−13.305	1	21.57	H
ATOM	4174	HD1	PHE C	113	−9.896	50.418	−12.615	1	27.62	H
ATOM	4175	HD2	PHE C	113	−7.594	47.231	−11.895	1	30.85	H
ATOM	4176	HE1	PHE C	113	−8.687	51.639	−11.085	1	30.77	H
ATOM	4177	HE2	PHE C	113	−6.382	48.452	−10.361	1	32.55	H
ATOM	4178	HZ	PHE C	113	−6.927	50.66	−9.953	1	31.39	H
ATOM	4179	N	PHE C	114	−9.339	46.858	−16.805	1	16.23	N
ATOM	4180	CA	PHE C	114	−9.855	45.885	−17.757	1	21.01	C
ATOM	4181	C	PHE C	114	−9.597	44.462	−17.277	1	23.07	C
ATOM	4182	O	PHE C	114	−8.447	44.064	−17.067	1	19.02	O
ATOM	4183	CB	PHE C	114	−9.229	46.114	−19.132	1	22.6	C
ATOM	4184	CG	PHE C	114	−9.646	47.407	−19.764	1	22.75	C
ATOM	4185	CD1	PHE C	114	−10.804	47.479	−20.517	1	26.86	C
ATOM	4186	CD2	PHE C	114	−8.895	48.556	−19.584	1	23.18	C
ATOM	4187	CE1	PHE C	114	−11.197	48.673	−21.094	1	30.06	C
ATOM	4188	CE2	PHE C	114	−9.283	49.751	−20.162	1	23.89	C
ATOM	4189	CZ	PHE C	114	−10.435	49.809	−20.914	1	22.95	C
ATOM	4190	H	PHE C	114	−8.525	47.092	−16.95	1	19.48	H
ATOM	4191	HA	PHE C	114	−10.815	46.003	−17.841	1	25.21	H
ATOM	4192	HB2	PHE C	114	−8.264	46.125	−19.039	1	27.12	H
ATOM	4193	HB3	PHE C	114	−9.496	45.393	−19.723	1	27.12	H
ATOM	4194	HD1	PHE C	114	−11.32	46.716	−20.642	1	32.23	H
ATOM	4195	HD2	PHE C	114	−8.116	48.521	−19.078	1	27.81	H
ATOM	4196	HE1	PHE C	114	−11.974	48.71	−21.603	1	36.07	H
ATOM	4197	HE2	PHE C	114	−8.769	50.517	−20.039	1	28.67	H
ATOM	4198	HZ	PHE C	114	−10.698	50.612	−21.303	1	27.54	H
ATOM	4199	N	ASP C	115	−10.676	43.702	−17.113	1	17.95	N
ATOM	4200	CA	ASP C	115	−10.596	42.336	−16.605	1	23.68	C
ATOM	4201	C	ASP C	115	−10.397	41.329	−17.734	1	26.5	C
ATOM	4202	O	ASP C	115	−10.405	40.12	−17.503	1	28.7	O
ATOM	4203	CB	ASP C	115	−11.856	41.988	−15.81	1	32.14	C
ATOM	4204	CG	ASP C	115	−13.112	42.022	−16.662	1	34.91	C
ATOM	4205	OD1	ASP C	115	−13.093	42.679	−17.724	1	35.65	O
ATOM	4206	OD2	ASP C	115	−14.118	41.395	−16.269	1	44.7	O1−
ATOM	4207	H	ASP C	115	−11.477	43.958	−17.291	1	21.53	H
ATOM	4208	HA	ASP C	115	−9.836	42.267	−16.006	1	28.42	H
ATOM	4209	HB2	ASP C	115	−11.764	41.093	−15.446	1	38.57	H
ATOM	4210	HB3	ASP C	115	−11.964	42.629	−15.09	1	38.57	H
ATOM	4211	N	GLU C	116	−10.227	41.832	−18.952	1	22.96	N
ATOM	4212	CA	GLU C	116	−9.886	40.989	−20.091	1	27.29	C
ATOM	4213	C	GLU C	116	−8.406	40.646	−20.029	1	28.42	C
ATOM	4214	O	GLU C	116	−7.556	41.538	−20.019	1	29.3	O
ATOM	4215	CB	GLU C	116	−10.212	41.689	−21.415	1	32.71	C
ATOM	4216	CG	GLU C	116	−11.703	41.836	−21.705	1	41.3	C
ATOM	4217	CD	GLU C	116	−12.404	42.802	−20.764	1	43.24	C
ATOM	4218	OE1	GLU C	116	−11.789	43.823	−20.383	1	32.76	O
ATOM	4219	OE2	GLU C	116	−13.572	42.536	−20.403	1	49.42	O1−
ATOM	4220	H	GLU C	116	−10.304	42.667	−19.146	1	27.55	H
ATOM	4221	HA	GLU C	116	−10.395	40.165	−20.046	1	32.74	H
ATOM	4222	HB2	GLU C	116	−9.827	42.579	−21.397	1	39.25	H
ATOM	4223	HB3	GLU C	116	−9.82	41.178	−22.14	1	39.25	H
ATOM	4224	HG2	GLU C	116	−11.816	42.166	−22.61	1	49.56	H
ATOM	4225	HG3	GLU C	116	−12.128	40.969	−21.614	1	49.56	H
ATOM	4226	N	SER C	117	−8.096	39.357	−19.979	1	18.99	N
ATOM	4227	CA	SER C	117	−6.709	38.922	−19.893	1	24.06	C
ATOM	4228	C	SER C	117	−6.009	39.087	−21.24	1	23.72	C
ATOM	4229	0	SER C	117	−6.42	38.498	−22.238	1	23.97	O
ATOM	4230	CB	SER C	117	−6.636	37.47	−19.425	1	24.23	C
ATOM	4231	OG	SER C	117	−5.313	37.131	−19.059	1	33.7	O
ATOM	4232	H	SER C	117	−8.669	38.716	−19.994	1	22.79	H
ATOM	4233	HA	SER C	117	−6.245	39.472	−19.243	1	28.88	H
ATOM	4234	HB2	SER C	117	−7.216	37.356	−18.656	1	29.08	H
ATOM	4235	HB3	SER C	117	−6.923	36.89	−20.147	1	29.08	H
ATOM	4236	HG	SER C	117	−5.052	37.628	−18.434	1	40.44	H
ATOM	4237	N	LYS C	118	−4.95	39.895	−21.255	1	19.67	N
ATOM	4238	CA	LYS C	118	−4.202	40.183	−22.476	1	18.97	C
ATOM	4239	C	LYS C	118	−2.705	40.264	−22.19	1	19.32	C
ATOM	4240	O	LYS C	118	−2.304	40.608	−21.081	1	17.06	O
ATOM	4241	CB	LYS C	118	−4.674	41.499	−23.096	1	20.06	C
ATOM	4242	CG	LYS C	118	−6.039	41.439	−23.756	1	24.89	C
ATOM	4243	CD	LYS C	118	−6.415	42.794	−24.345	1	27.05	C
ATOM	4244	CE	LYS C	118	−7.689	42.712	−25.171	1	30.29	C
ATOM	4245	NZ	LYS C	118	−8.838	42.217	−24.367	1	41.79	N1+
ATOM	4246	H	LYS C	118	−4.642	40.295	−20.559	1	23.6	H
ATOM	4247	HA	LYS C	118	−4.351	39.472	−23.119	1	22.76	H
ATOM	4248	HB2	LYS C	118	−4.715	42.172	−22.399	1	24.07	H
ATOM	4249	HB3	LYS C	118	−4.034	41.769	−23.773	1	24.07	H
ATOM	4250	HG2	LYS C	118	−6.022	40.787	−24.474	1	29.87	H
ATOM	4251	HG3	LYS C	118	−6.706	41.196	−23.095	1	29.87	H
ATOM	4252	HD2	LYS C	118	−6.561	43.426	−23.624	1	32.46	H
ATOM	4253	HD3	LYS C	118	−5.699	43.102	−24.921	1	32.46	H
ATOM	4254	HE2	LYS C	118	−7.91	43.596	−25.504	1	36.35	H
ATOM	4255	HE3	LYS C	118	−7.55	42.1	−25.91	1	36.35	H
ATOM	4256	HZ1	LYS C	118	−8.661	41.403	−24.053	1	50.14	H
ATOM	4257	HZ2	LYS C	118	−8.988	42.765	−23.682	1	50.14	H
ATOM	4258	HZ3	LYS C	118	−9.569	42.179	−24.873	1	50.14	H
ATOM	4259	N	ASN C	119	−1.876	39.965	−23.186	1	16.38	N
ATOM	4260	CA	ASN C	119	−0.438	40.141	−23.016	1	19.02	C
ATOM	4261	C	ASN C	119	−0.135	41.64	−23.019	1	17.17	C
ATOM	4262	O	ASN C	119	−1.03	42.453	−23.271	1	15.21	O
ATOM	4263	CB	ASN C	119	0.354	39.374	−24.095	1	16.08	C
ATOM	4264	CG	ASN C	119	0.249	39.985	−25.491	1	21.42	C
ATOM	4265	OD1	ASN C	119	0.176	41.202	−25.669	1	20.88	O
ATOM	4266	ND2	ASN C	119	0.267	39.119	−26.5	1	28.85	N
ATOM	4267	H	ASN C	119	−2.115	39.664	−23.956	1	19.65	H
ATOM	4268	HA	ASN C	119	−0.179	39.788	−22.151	1	22.82	H
ATOM	4269	HB2	ASN C	119	1.291	39.363	−23.846	1	19.3	H
ATOM	4270	HB3	ASN C	119	0.016	38.466	−24.144	1	19.3	H
ATOM	4271	HD21	ASN C	119	0.211	39.402	−27.311	1	34.62	H
ATOM	4272	HD22	ASN C	119	0.334	38.276	−26.343	1	34.62	H
ATOM	4273	N	TRP C	120	1.108	42.013	−22.734	1	17.45	N
ATOM	4274	CA	TRP C	120	1.443	43.427	−22.571	1	16.39	C
ATOM	4275	C	TRP C	120	1.229	44.216	−23.861	1	19.16	C
ATOM	4276	O	TRP C	120	0.768	45.36	−23.822	1	20.05	O
ATOM	4277	CB	TRP C	120	2.888	43.592	−22.098	1	15.72	C
ATOM	4278	CG	TRP C	120	3.216	45.005	−21.718	1	18.6	C
ATOM	4279	CD1	TRP C	120	3.152	45.554	−20.47	1	18.56	C
ATOM	4280	CD2	TRP C	120	3.652	46.053	−22.593	1	18.79	C
ATOM	4281	NE1	TRP C	120	3.518	46.876	−20.514	1	17.94	N
ATOM	4282	CE2	TRP C	120	3.83	47.208	−21.805	1	20.55	C
ATOM	4283	CE3	TRP C	120	3.903	46.128	−23.966	1	23.33	C
ATOM	4284	CZ2	TRP C	120	4.251	48.42	−22.342	1	21.4	C
ATOM	4285	CZ3	TRP C	120	4.321	47.334	−24.497	1	19.62	C
ATOM	4286	CH2	TRP C	120	4.492	48.463	−23.687	1	24.59	C
ATOM	4287	H	TRP C	120	1.771	41.475	−22.631	1	20.94	H
ATOM	4288	HA	TRP C	120	0.864	43.807	−21.892	1	19.67	H
ATOM	4289	HB2	TRP C	120	3.032	43.032	−21.319	1	18.86	H
ATOM	4290	HB3	TRP C	120	3.487	43.327	−22.813	1	18.86	H
ATOM	4291	HD1	TRP C	120	2.895	45.098	−19.701	1	22.28	H
ATOM	4292	HE1	TRP C	120	3.55	47.408	−19.839	1	21.53	H
ATOM	4293	HE3	TRP C	120	3.791	45.383	−24.511	1	28	H
ATOM	4294	HZ2	TRP C	120	4.366	49.172	−21.806	1	25.69	H
ATOM	4295	HZ3	TRP C	120	4.493	47.396	−25.409	1	23.55	H
ATOM	4296	HH2	TRP C	120	4.776	49.26	−24.072	1	29.5	H
ATOM	4297	N	TYR C	121	1.555	43.605	−24.998	1	17.25	N
ATOM	4298	CA	TYR C	121	1.432	44.28	−26.289	1	19.29	C
ATOM	4299	C	TYR C	121	−0.035	44.502	−26.645	1	19.51	C
ATOM	4300	O	TYR C	121	−0.406	45.554	−27.164	1	22.89	O
ATOM	4301	CB	TYR C	121	2.124	43.472	−27.392	1	22.07	C
ATOM	4302	CG	TYR C	121	3.47	42.922	−26.983	1	18.97	C
ATOM	4303	CD1	TYR C	121	4.582	43.748	−26.897	1	21.63	C
ATOM	4304	CD2	TYR C	121	3.627	41.577	−26.675	1	18.97	C
ATOM	4305	CE1	TYR C	121	5.812	43.25	−26.517	1	22.33	C
ATOM	4306	CE2	TYR C	121	4.853	41.07	−26.296	1	21.4	C
ATOM	4307	CZ	TYR C	121	5.939	41.91	−26.216	1	21.86	C
ATOM	4308	OH	TYR C	121	7.161	41.408	−25.84	1	22.74	O
ATOM	4309	H	TYR C	121	1.85	42.799	−25.049	1	20.71	H
ATOM	4310	HA	TYR C	121	1.863	45.148	−26.236	1	23.15	H
ATOM	4311	HB2	TYR C	121	1.558	42.722	−27.633	1	26.49	H
ATOM	4312	HB3	TYR C	121	2.259	44.044	−28.163	1	26.49	H
ATOM	4313	HD1	TYR C	121	4.496	44.652	−27.097	1	25.95	H
ATOM	4314	HD2	TYR C	121	2.893	41.008	−26.726	1	22.76	H
ATOM	4315	HE1	TYR C	121	6.55	43.815	−26.464	1	26.8	H
ATOM	4316	HE2	TYR C	121	4.944	40.167	−26.092	1	25.68	H
ATOM	4317	HH	TYR C	121	7.734	42.021	−25.835	1	27.29	H
ATOM	4318	N	GLU C	122	−0.864	43.503	−26.363	1	19.03	N
ATOM	4319	CA	GLU C	122	−2.296	43.606	−26.607	1	20.24	C
ATOM	4320	C	GLU C	122	−2.911	44.657	−25.688	1	22.15	C
ATOM	4321	O	GLU C	122	−3.781	45.424	−26.098	1	21.67	O
ATOM	4322	CB	GLU C	122	−2.969	42.249	−26.399	1	23.32	C
ATOM	4323	CG	GLU C	122	−2.577	41.198	−27.442	1	28.93	C
ATOM	4324	CD	GLU C	122	−3.051	39.794	−27.089	1	31.55	C
ATOM	4325	OE1	GLU C	122	−3.184	39.484	−25.884	1	26.49	O
ATOM	4326	OE2	GLU C	122	−3.289	38.996	−28.023	1	36.3	O1−
ATOM	4327	H	GLU C	122	−0.619	42.75	−26.028	1	22.84	H
ATOM	4328	HA	GLU C	122	−2.445	43.881	−27.525	1	24.29	H
ATOM	4329	HB2	GLU C	122	−2.72	41.907	−25.526	1	27.98	H
ATOM	4330	HB3	GLU C	122	−3.931	42.366	−26.444	1	27.98	H
ATOM	4331	HG2	GLU C	122	−2.97	41.44	−28.295	1	34.71	H
ATOM	4332	HG3	GLU C	122	−1.61	41.176	−27.517	1	34.71	H
ATOM	4333	N	SER C	123	−2.442	44.696	−24.446	1	20.16	N
ATOM	4334	CA	SER C	123	−2.934	45.664	−23.473	1	21.59	C
ATOM	4335	C	SER C	123	−2.539	47.085	−23.865	1	20.7	C
ATOM	4336	O	SER C	123	−3.328	48.019	−23.717	1	19.9	O
ATOM	4337	CB	SER C	123	−2.405	45.335	−22.08	1	19.87	C
ATOM	4338	OG	SER C	123	−2.871	44.07	−21.655	1	17.57	O
ATOM	4339	H	SER C	123	−1.836	44.169	−24.14	1	24.19	H
ATOM	4340	HA	SER C	123	−3.903	45.619	−23.445	1	25.91	H
ATOM	4341	HB2	SER C	123	−1.436	45.323	−22.105	1	23.85	H
ATOM	4342	HB3	SER C	123	−2.713	46.011	−21.457	1	23.85	H
ATOM	4343	HG	SER C	123	−2.612	43.475	−22.188	1	21.09	H
ATOM	4344	N	GLN C	124	−1.318	47.244	−24.366	1	24.47	N
ATOM	4345	CA	GLN C	124	−0.843	48.55	−24.805	1	22.72	C
ATOM	4346	C	GLN C	124	−1.706	49.08	−25.946	1	24.57	C
ATOM	4347	O	GLN C	124	−2.072	50.256	−25.962	1	20.57	O
ATOM	4348	CB	GLN C	124	0.619	48.478	−25.256	1	26.56	C
ATOM	4349	CG	GLN C	124	1.218	49.843	−25.591	1	36.95	C
ATOM	4350	CD	GLN C	124	2.42	49.764	−26.513	1	46.63	C
ATOM	4351	OE1	GLN C	124	2.512	48.882	−27.367	1	51.66	O
ATOM	4352	NE2	GLN C	124	3.351	50.695	−26.344	1	54.16	N
ATOM	4353	H	GLN C	124	−0.745	46.61	−24.462	1	29.36	H
ATOM	4354	HA	GLN C	124	−0.901	49.176	−24.066	1	27.27	H
ATOM	4355	HB2	GLN C	124	1.148	48.087	−24.543	1	31.87	H
ATOM	4356	HB3	GLN C	124	0.675	47.925	−26.05	1	31.87	H
ATOM	4357	HG2	GLN C	124	0.542	50.384	−26.029	1	44.35	H
ATOM	4358	HG3	GLN C	124	1.501	50.272	−24.769	1	44.35	H
ATOM	4359	HE21	GLN C	124	4.053	50.696	−26.84	1	64.99	H
ATOM	4360	HE22	GLN C	124	3.253	51.297	−25.737	1	64.99	H
ATOM	4361	N	ALA C	125	−2.013	48.209	−26.905	1	22.47	N
ATOM	4362	CA	ALA C	125	−2.833	48.589	−28.053	1	26.65	C
ATOM	4363	C	ALA C	125	−4.243	48.953	−27.612	1	27.08	C
ATOM	4364	O	ALA C	125	−4.863	49.867	−28.162	1	28.57	O
ATOM	4365	CB	ALA C	125	−2.877	47.464	−29.074	1	20.86	C
ATOM	4366	H	ALA C	125	−1.758	47.388	−26.914	1	26.96	H
ATOM	4367	HA	ALA C	125	−2.44	49.368	−28.479	1	31.98	H
ATOM	4368	HB1	ALA C	125	−3.426	47.741	−29.825	1	25.03	H
ATOM	4369	HB2	ALA C	125	−1.974	47.276	−29.375	1	25.03	H
ATOM	4370	HB3	ALA C	125	−3.258	46.676	−28.658	1	25.03	H
ATOM	4371	N	SER C	126	−4.747	48.225	−26.622	1	19.59	N
ATOM	4372	CA	SER C	126	−6.082	48.473	−26.088	1	26.3	C
ATOM	4373	C	SER C	126	−6.193	49.891	−25.531	1	26.98	C
ATOM	4374	O	SER C	126	−7.138	50.616	−25.844	1	26.2	O
ATOM	4375	CB	SER C	126	−6.419	47.449	−25.003	1	24.52	C
ATOM	4376	OG	SER C	126	−7.657	47.745	−24.384	1	25.71	O
ATOM	4377	H	SER C	126	−4.333	47.575	−26.239	1	23.51	H
ATOM	4378	HA	SER C	126	−6.731	48.379	−26.802	1	31.56	H
ATOM	4379	HB2	SER C	126	−6.472	46.569	−25.407	1	29.43	H
ATOM	4380	HB3	SER C	126	−5.72	47.462	−24.33	1	29.43	H
ATOM	4381	HG	SER C	126	−7.826	47.174	−23.792	1	30.85	H
ATOM	4382	N	CYS C	127	−5.218	50.285	−24.717	1	24.31	N
ATOM	4383	CA	CYS C	127	−5.209	51.616	−24.121	1	23.85	C
ATOM	4384	C	CYS C	127	−5.053	52.705	−25.182	1	28.4	C
ATOM	4385	O	CYS C	127	−5.731	53.734	−25.127	1	25.1	O
ATOM	4386	CB	CYS C	127	−4.088	51.731	−23.086	1	21.86	C
ATOM	4387	SG	CYS C	127	−4.254	50.602	−21.682	1	18.33	S
ATOM	4388	H	CYS C	127	−4.546	49.796	−24.493	1	29.17	H
ATOM	4389	HA	CYS C	127	−6.053	51.762	−23.665	1	28.62	H
ATOM	4390	HB2	CYS C	127	−3.243	51.539	−23.521	1	26.23	H
ATOM	4391	HB3	CYS C	127	−4.079	52.636	−22.737	1	26.23	H
ATOM	4392	N	MET C	128	−4.159	52.476	−26.142	1	24.31	N
ATOM	4393	CA	MET C	128	−3.917	53.445	−27.21	1	28.72	C
ATOM	4394	C	MET C	128	−5.173	53.665	−28.049	1	28.9	C
ATOM	4395	O	MET C	128	−5.436	54.776	−28.504	1	34.94	O
ATOM	4396	CB	MET C	128	−2.77	52.985	−28.114	1	29.76	C
ATOM	4397	CG	MET C	128	−1.377	53.258	−27.565	1	41.22	C
ATOM	4398	SD	MET C	128	−0.084	53.092	−28.823	1	57.79	S
ATOM	4399	CE	MET C	128	−0.259	51.366	−29.269	1	79.41	C
ATOM	4400	H	MET C	128	−3.679	51.765	−26.199	1	29.18	H
ATOM	4401	HA	MET C	128	−3.658	54.289	−26.81	1	34.46	H
ATOM	4402	HB2	MET C	128	−2.848	52.028	−28.251	1	35.71	H
ATOM	4403	HB3	MET C	128	−2.844	53.443	−28.966	1	35.71	H
ATOM	4404	HG2	MET C	128	−1.345	54.165	−27.22	1	49.47	H
ATOM	4405	HG3	MET C	128	−1.187	52.626	−26.854	1	49.47	H
ATOM	4406	HE1	MET C	128	0.395	51.149	−29.952	1	95.3	H
ATOM	4407	HE2	MET C	128	−0.109	50.82	−28.481	1	95.3	H
ATOM	4408	HE3	MET C	128	−1.155	51.218	−29.609	1	95.3	H
ATOM	4409	N	SER C	129	−5.945	52.601	−28.246	1	29.07	N
ATOM	4410	CA	SER C	129	−7.157	52.672	−29.055	1	32	C
ATOM	4411	C	SER C	129	−8.256	53.469	−28.358	1	36.56	C
ATOM	4412	O	SER C	129	−9.307	53.735	−28.945	1	32.22	O
ATOM	4413	CB	SER C	129	−7.669	51.267	−29.377	1	33.16	C
ATOM	4414	OG	SER C	129	−8.267	50.67	−28.237	1	33.58	O
ATOM	4415	H	SER C	129	−5.788	51.821	−27.92	1	34.88	H
ATOM	4416	HA	SER C	129	−6.952	53.115	−29.893	1	38.4	H
ATOM	4417	HB2	SER C	129	−8.329	51.325	−30.085	1	39.79	H
ATOM	4418	HB3	SER C	129	−6.922	50.718	−29.664	1	39.79	H
ATOM	4419	HG	SER C	129	−7.706	50.613	−27.615	1	40.3	H
ATOM	4420	N	GLN C	130	−8.01	53.834	−27.102	1	33.51	N
ATOM	4421	CA	GLN C	130	−8.946	54.642	−26.331	1	30.27	C
ATOM	4422	C	GLN C	130	−8.314	55.976	−25.955	1	26.64	C
ATOM	4423	O	GLN C	130	−8.73	56.622	−24.995	1	31.87	O
ATOM	4424	CB	GLN C	130	−9.393	53.881	−25.082	1	30.65	C
ATOM	4425	CG	GLN C	130	−10.037	52.545	−25.414	1	34.01	C
ATOM	4426	CD	GLN C	130	−10.477	51.776	−24.191	1	33.95	C
ATOM	4427	OE1	GLN C	130	−11.212	52.29	−23.347	1	40.96	O
ATOM	4428	NE2	GLN C	130	−10.033	50.529	−24.089	1	34.2	N
ATOM	4429	H	GLN C	130	−7.297	53.622	−26.67	1	40.22	H
ATOM	4430	HA	GLN C	130	−9.731	54.822	−26.872	1	36.32	H
ATOM	4431	HB2	GLN C	130	−8.62	53.711	−24.521	1	36.78	H
ATOM	4432	HB3	GLN C	130	−10.043	54.416	−24.601	1	36.78	H
ATOM	4433	HG2	GLN C	130	−10.819	52.701	−25.966	1	40.81	H
ATOM	4434	HG3	GLN C	130	−9.396	51.998	−25.896	1	40.81	H
ATOM	4435	HE21	GLN C	130	−10.254	50.047	−23.411	1	41.04	H
ATOM	4436	HE22	GLN C	130	−9.523	50.203	−24.7	1	41.04	H
ATOM	4437	N	ASN C	131	−7.312	56.382	−26.73	1	25.72	N
ATOM	4438	CA	ASN C	131	−6.593	57.631	−26.495	1	31.52	C
ATOM	4439	C	ASN C	131	−6.008	57.676	−25.091	1	30.51	C
ATOM	4440	O	ASN C	131	−5.996	58.719	−24.433	1	30.75	O
ATOM	4441	CB	ASN C	131	−7.512	58.833	−26.721	1	40	C
ATOM	4442	CG	ASN C	131	−6.739	60.121	−26.931	1	45.49	C
ATOM	4443	OD1	ASN C	131	−6.12	60.32	−27.975	1	53.22	O
ATOM	4444	ND2	ASN C	131	−6.769	61.001	−25.937	1	44.21	N
ATOM	4445	H	ASN C	131	−7.025	55.944	−27.412	1	30.86	H
ATOM	4446	HA	ASN C	131	−5.859	57.695	−27.126	1	37.83	H
ATOM	4447	HB2	ASN C	131	−8.053	58.675	−27.511	1	48	H
ATOM	4448	HB3	ASN C	131	−8.082	58.947	−25.945	1	48	H
ATOM	4449	HD21	ASN C	131	−6.346	61.746	−26.009	1	53.05	H
ATOM	4450	HD22	ASN C	131	−7.211	60.826	−25.22	1	53.05	H
ATOM	4451	N	ALA C	132	−5.522	56.526	−24.641	1	27.31	N
ATOM	4452	CA	ALA C	132	−4.952	56.397	−23.311	1	24.35	C
ATOM	4453	C	ALA C	132	−3.654	55.604	−23.376	1	22.93	C
ATOM	4454	O	ALA C	132	−3.175	55.264	−24.456	1	22.28	O
ATOM	4455	CB	ALA C	132	−5.946	55.724	−22.377	1	24.1	C
ATOM	4456	H	ALA C	132	−5.512	55.796	−25.096	1	32.77	H
ATOM	4457	HA	ALA C	132	−4.753	57.279	−22.96	1	29.22	H
ATOM	4458	HB1	ALA C	132	−5.548	55.647	−21.496	1	28.92	H
ATOM	4459	HB2	ALA C	132	−6.75	56.264	−22.331	1	28.92	H
ATOM	4460	HB3	ALA C	132	−6.157	54.843	−22.724	1	28.92	H
ATOM	4461	N	SER C	133	−3.086	55.317	−22.211	1	23.85	N
ATOM	4462	CA	SER C	133	−1.908	54.47	−22.123	1	19.49	C
ATOM	4463	C	SER C	133	−2.035	53.561	−20.913	1	19.76	C
ATOM	4464	O	SER C	133	−2.954	53.714	−20.106	1	21.65	O
ATOM	4465	CB	SER C	133	−0.637	55.315	−22.035	1	28.62	C
ATOM	4466	OG	SER C	133	−0.593	56.041	−20.822	1	30.86	O
ATOM	4467	H	SER C	133	−3.368	55.604	−21.451	1	28.62	H
ATOM	4468	HA	SER C	133	−1.851	53.916	−22.917	1	23.39	H
ATOM	4469	HB2	SER C	133	0.135	54.73	−22.081	1	34.34	H
ATOM	4470	HB3	SER C	133	−0.622	55.94	−22.777	1	34.34	H
ATOM	4471	HG	SER C	133	−1.256	56.554	−20.769	1	37.04	H
ATOM	4472	N	LEU C	134	−1.131	52.597	−20.799	1	15.3	N
ATOM	4473	CA	LEU C	134	−1.085	51.753	−19.618	1	16.31	C
ATOM	4474	C	LEU C	134	−0.722	52.605	−18.413	1	18.61	C
ATOM	4475	O	LEU C	134	−0.102	53.66	−18.558	1	17.38	O
ATOM	4476	CB	LEU C	134	−0.082	50.615	−19.8	1	18.05	C
ATOM	4477	CG	LEU C	134	−0.545	49.502	−20.739	1	18.46	C
ATOM	4478	CD1	LEU C	134	0.622	48.613	−21.151	1	18.54	C
ATOM	4479	CD2	LEU C	134	−1.633	48.677	−20.07	1	13.57	C
ATOM	4480	H	LEU C	134	−0.535	52.413	−21.391	1	18.36	H
ATOM	4481	HA	LEU C	134	−1.961	51.366	−19.465	1	19.57	H
ATOM	4482	HB2	LEU C	134	0.74	50.982	−20.162	1	21.66	H
ATOM	4483	HB3	LEU C	134	0.094	50.215	−18.934	1	21.66	H
ATOM	4484	HG	LEU C	134	−0.919	49.899	−21.541	1	22.15	H
ATOM	4485	HD11	LEU C	134	0.296	47.919	−21.745	1	22.25	H
ATOM	4486	HD12	LEU C	134	1.285	49.154	−21.608	1	22.25	H
ATOM	4487	HD13	LEU C	134	1.011	48.214	−20.357	1	22.25	H
ATOM	4488	HD21	LEU C	134	−1.916	47.976	−20.678	1	16.29	H
ATOM	4489	HD22	LEU C	134	−1.278	48.287	−19.256	1	16.29	H
ATOM	4490	HD23	LEU C	134	−2.383	49.256	−19.859	1	16.29	H
ATOM	4491	N	LEU C	135	−1.122	52.145	−17.232	1	17.61	N
ATOM	4492	CA	LEU C	135	−0.861	52.863	−15.99	1	16.82	C
ATOM	4493	C	LEU C	135	0.574	53.365	−15.907	1	17.04	C
ATOM	4494	O	LEU C	135	1.521	52.614	−16.145	1	17.43	O
ATOM	4495	CB	LEU C	135	−1.16	51.962	−14.792	1	13.74	C
ATOM	4496	CG	LEU C	135	−0.816	52.517	−13.409	1	13.56	C
ATOM	4497	CD1	LEU C	135	−1.668	53.736	−13.089	1	14.51	C
ATOM	4498	CD2	LEU C	135	−0.994	51.438	−12.348	1	14.41	C
ATOM	4499	H	LEU C	135	−1.553	51.409	−17.123	1	21.14	H
ATOM	4500	HA	LEU C	135	−1.45	53.632	−15.941	1	20.18	H
ATOM	4501	HB2	LEU C	135	−2.109	51.762	−14.793	1	16.49	H
ATOM	4502	HB3	LEU C	135	−0.66	51.138	−14.901	1	16.49	H
ATOM	4503	HG	LEU C	135	0.114	52.793	−13.402	1	16.27	H
ATOM	4504	HD11	LEU C	135	−1.429	54.066	−12.209	1	17.41	H
ATOM	4505	HD12	LEU C	135	−1.502	54.421	−13.756	1	17.41	H
ATOM	4506	HD13	LEU C	135	−2.604	53.48	−13.104	1	17.41	H
ATOM	4507	HD21	LEU C	135	−0.772	51.81	−11.48	1	17.29	H
ATOM	4508	HD22	LEU C	135	−1.917	51.139	−12.354	1	17.29	H
ATOM	4509	HD23	LEU C	135	−0.404	50.695	−12.551	1	17.29	H
ATOM	4510	N	LYS C	136	0.716	54.65	−15.601	1	17.22	N
ATOM	4511	CA	LYS C	136	2	55.223	−15.224	1	18.54	C
ATOM	4512	C	LYS C	136	1.937	55.661	−13.766	1	20.47	C
ATOM	4513	O	LYS C	136	1.05	56.424	−13.383	1	19.64	O
ATOM	4514	CB	LYS C	136	2.365	56.409	−16.117	1	20.46	C
ATOM	4515	CG	LYS C	136	3.646	57.121	−15.689	1	23.01	C
ATOM	4516	CD	LYS C	136	3.99	58.278	−16.612	1	23.3	C
ATOM	4517	CE	LYS C	136	5.219	59.029	−16.123	1	27.96	C
ATOM	4518	NZ	LYS C	136	5.543	60.212	−16.968	1	28.81	N1+
ATOM	4519	H	LYS C	136	0.072	55.219	−15.605	1	20.67	H
ATOM	4520	HA	LYS C	136	2.692	54.549	−15.312	1	22.25	H
ATOM	4521	HB2	LYS C	136	2.49	56.091	−17.025	1	24.55	H
ATOM	4522	HB3	LYS C	136	1.642	57.055	−16.09	1	24.55	H
ATOM	4523	HG2	LYS C	136	3.53	57.473	−14.792	1	27.61	H
ATOM	4524	HG3	LYS C	136	4.382	56.49	−15.708	1	27.61	H
ATOM	4525	HD2	LYS C	136	4.175	57.936	−17.5	1	27.96	H
ATOM	4526	HD3	LYS C	136	3.245	58.899	−16.639	1	27.96	H
ATOM	4527	HE2	LYS C	136	5.061	59.341	−15.218	1	33.55	H
ATOM	4528	HE3	LYS C	136	5.983	58.431	−16.14	1	33.55	H
ATOM	4529	HZ1	LYS C	136	5.701	59.954	−17.805	1	34.57	H
ATOM	4530	HZ2	LYS C	136	4.86	60.783	−16.965	1	34.57	H
ATOM	4531	HZ3	LYS C	136	6.265	60.623	−16.65	1	34.57	H
ATOM	4532	N	VAL C	137	2.879	55.174	−12.962	1	17.55	N
ATOM	4533	CA	VAL C	137	2.946	55.507	−11.54	1	20.81	C
ATOM	4534	C	VAL C	137	3.952	56.623	−11.309	1	21.28	C
ATOM	4535	O	VAL C	137	5.166	56.402	−11.4	1	21.39	O
ATOM	4536	CB	VAL C	137	3.34	54.286	−10.685	1	17.34	C
ATOM	4537	CG1	VAL C	137	3.489	54.674	−9.218	1	17.08	C
ATOM	4538	CG2	VAL C	137	2.308	53.18	−10.832	1	19.83	C
ATOM	4539	H	VAL C	137	3.501	54.639	−13.221	1	21.06	H
ATOM	4540	HA	VAL C	137	2.075	55.816	−11.243	1	24.98	H
ATOM	4541	HB	VAL C	137	4.194	53.945	−10.994	1	20.81	H
ATOM	4542	HG11	VAL C	137	3.737	53.887	−8.708	1	20.5	H
ATOM	4543	HG12	VAL C	137	4.179	55.351	−9.14	1	20.5	H
ATOM	4544	HG13	VAL C	137	2.643	55.024	−8.897	1	20.5	H
ATOM	4545	HG21	VAL C	137	2.576	52.424	−10.287	1	23.8	H
ATOM	4546	HG22	VAL C	137	1.446	53.512	−10.537	1	23.8	H
ATOM	4547	HG23	VAL C	137	2.26	52.915	−11.764	1	23.8	H
ATOM	4548	N	TYR C	138	3.447	57.812	−10.992	1	20.38	N
ATOM	4549	CA	TYR C	138	4.298	58.989	−10.848	1	21.11	C
ATOM	4550	C	TYR C	138	4.204	59.608	−9.457	1	24.17	C
ATOM	4551	O	TYR C	138	5.071	60.393	−9.071	1	24.32	O
ATOM	4552	CB	TYR C	138	3.94	60.037	−11.906	1	22.43	C
ATOM	4553	CG	TYR C	138	2.622	60.739	−11.663	1	20.09	C
ATOM	4554	CD1	TYR C	138	1.442	60.245	−12.197	1	21.54	C
ATOM	4555	CD2	TYR C	138	2.56	61.899	−10.899	1	24.15	C
ATOM	4556	CE1	TYR C	138	0.238	60.882	−11.978	1	23.42	C
ATOM	4557	CE2	TYR C	138	1.361	62.542	−10.673	1	24.55	C
ATOM	4558	CZ	TYR C	138	0.204	62.029	−11.214	1	24.76	C
ATOM	4559	OH	TYR C	138	−0.991	62.663	−10.994	1	25.68	O
ATOM	4560	H	TYR C	138	2.612	57.965	−10.855	1	24.46	H
ATOM	4561	HA	TYR C	138	5.221	58.726	−10.992	1	25.34	H
ATOM	4562	HB2	TYR C	138	4.636	60.712	−11.923	1	26.92	H
ATOM	4563	HB3	TYR C	138	3.887	59.6	−12.77	1	26.92	H
ATOM	4564	HD1	TYR C	138	1.462	59.471	−12.712	1	25.85	H
ATOM	4565	HD2	TYR C	138	3.341	62.246	−10.531	1	28.98	H
ATOM	4566	HE1	TYR C	138	−0.546	60.538	−12.342	1	28.11	H
ATOM	4567	HE2	TYR C	138	1.334	63.316	−10.159	1	29.46	H
ATOM	4568	HH	TYR C	138	−0.872	63.344	−10.517	1	30.82	H
ATOM	4569	N	SER C	139	3.16	59.265	−8.704	1	20.17	N
ATOM	4570	CA	SER C	139	2.98	59.837	−7.369	1	25.07	C
ATOM	4571	C	SER C	139	2.203	58.946	−6.407	1	22.13	C
ATOM	4572	0	SER C	139	1.051	58.586	−6.664	1	19.25	O
ATOM	4573	CB	SER C	139	2.267	61.184	−7.468	1	26.51	C
ATOM	4574	OG	SER C	139	1.936	61.668	−6.178	1	27.3	O
ATOM	4575	H	SER C	139	2.547	58.709	−8.939	1	24.21	H
ATOM	4576	HA	SER C	139	3.854	59.995	−6.98	1	30.08	H
ATOM	4577	HB2	SER C	139	2.854	61.821	−7.905	1	31.82	H
ATOM	4578	HB3	SER C	139	1.453	61.074	−7.984	1	31.82	H
ATOM	4579	HG	SER C	139	1.545	62.408	−6.24	1	32.76	H
ATOM	4580	N	LYS C	140	2.828	58.62	−5.28	1	15.89	N
ATOM	4581	CA	LYS C	140	2.167	57.822	−4.254	1	23.7	C
ATOM	4582	C	LYS C	140	0.968	58.551	−3.655	1	24.9	C
ATOM	4583	O	LYS C	140	−0.012	57.922	−3.258	1	26.09	O
ATOM	4584	CB	LYS C	140	3.15	57.456	−3.142	1	28.92	C
ATOM	4585	CG	LYS C	140	4.057	56.282	−3.47	1	29.54	C
ATOM	4586	CD	LYS C	140	4.867	55.875	−2.252	1	37.47	C
ATOM	4587	CE	LYS C	140	5.648	54.596	−2.489	1	37.64	C
ATOM	4588	NZ	LYS C	140	6.295	54.118	−1.233	1	49.87	N1+
ATOM	4589	H	LYS C	140	3.634	58.848	−5.085	1	19.07	H
ATOM	4590	HA	LYS C	140	1.847	56.998	−4.653	1	28.44	H
ATOM	4591	HB2	LYS C	140	3.715	58.224	−2.962	1	34.7	H
ATOM	4592	HB3	LYS C	140	2.646	57.226	−2.346	1	34.7	H
ATOM	4593	HG2	LYS C	140	3.517	55.525	−3.746	1	35.45	H
ATOM	4594	HG3	LYS C	140	4.671	56.536	−4.177	1	35.45	H
ATOM	4595	HD2	LYS C	140	5.499	56.581	−2.04	1	44.96	H
ATOM	4596	HD3	LYS C	140	4.267	55.729	−1.504	1	44.96	H
ATOM	4597	HE2	LYS C	140	5.045	53.905	−2.803	1	45.16	H
ATOM	4598	HE3	LYS C	140	6.343	54.762	−3.145	1	45.16	H
ATOM	4599	HZ1	LYS C	140	6.748	53.368	−1.391	1	59.85	H
ATOM	4600	HZ2	LYS C	140	6.857	54.736	−0.926	1	59.85	H
ATOM	4601	HZ3	LYS C	140	5.676	53.957	−0.614	1	59.85	H
ATOM	4602	N	GLU C	141	1.046	59.876	−3.593	1	24.55	N
ATOM	4603	CA	GLU C	141	−0.002	60.674	−2.963	1	26.23	C
ATOM	4604	C	GLU C	141	−1.169	60.917	−3.914	1	24.95	C
ATOM	4605	O	GLU C	141	−2.327	60.758	−3.534	1	21.89	O
ATOM	4606	CB	GLU C	141	0.559	62.01	−2.474	1	26.15	C
ATOM	4607	CG	GLU C	141	1.543	61.885	−1.314	1	34.78	C
ATOM	4608	CD	GLU C	141	2.855	61.219	−1.707	1	37.55	C
ATOM	4609	OE1	GLU C	141	3.227	61.278	−2.899	1	33.99	O
ATOM	4610	OE2	GLU C	141	3.514	60.634	−0.82	1	45.19	O1−
ATOM	4611	H	GLU C	141	1.698	60.339	−3.91	1	29.46	H
ATOM	4612	HA	GLU C	141	−0.342	60.193	−2.192	1	31.47	H
ATOM	4613	HB2	GLU C	141	1.022	62.442	−3.209	1	31.39	H
ATOM	4614	HB3	GLU C	141	−0.178	62.568	−2.178	1	31.39	H
ATOM	4615	HG2	GLU C	141	1.747	62.772	−0.978	1	41.74	H
ATOM	4616	HG3	GLU C	141	1.136	61.352	−0.613	1	41.74	H
ATOM	4617	N	ASP C	142	−0.867	61.296	−5.152	1	22.41	N
ATOM	4618	CA	ASP C	142	−1.915	61.567	−6.129	1	21.49	C
ATOM	4619	C	ASP C	142	−2.56	60.282	−6.633	1	21.91	C
ATOM	4620	0	ASP C	142	−3.686	60.3	−7.128	1	24.05	O
ATOM	4621	CB	ASP C	142	−1.357	62.369	−7.307	1	24.21	C
ATOM	4622	CG	ASP C	142	−0.908	63.76	−6.901	1	29.23	C
ATOM	4623	OD1	ASP C	142	−1.248	64.193	−5.776	1	30.52	O
ATOM	4624	OD2	ASP C	142	−0.223	64.424	−7.707	1	33.69	O1−
ATOM	4625	H	ASP C	142	−0.067	61.403	−5.45	1	26.89	H
ATOM	4626	HA	ASP C	142	−2.606	62.101	−5.707	1	25.79	H
ATOM	4627	HB2	ASP C	142	−0.59	61.901	−7.674	1	29.05	H
ATOM	4628	HB3	ASP C	142	−2.046	62.46	−7.983	1	29.05	H
ATOM	4629	N	GLN C	143	−1.849	59.167	−6.501	1	17.21	N
ATOM	4630	CA	GLN C	143	−2.357	57.882	−6.969	1	20.06	C
ATOM	4631	C	GLN C	143	−2.424	56.89	−5.819	1	19.18	C
ATOM	4632	O	GLN C	143	−2.183	55.696	−5.994	1	17.46	O
ATOM	4633	CB	GLN C	143	−1.479	57.342	−8.097	1	18.97	C
ATOM	4634	CG	GLN C	143	−1.248	58.349	9.217	1	17.93	C
ATOM	4635	CD	GLN C	143	−0.285	57.837	−10.27	1	21.93	C
ATOM	4636	OE1	GLN C	143	0.917	57.724	−10.024	1	19.88	O
ATOM	4637	NE2	GLN C	143	−0.808	57.52	−11.45	1	17.07	N
ATOM	4638	H	GLN C	143	−1.069	59.128	−6.143	1	20.65	H
ATOM	4639	HA	GLN C	143	−3.255	58.002	−7.317	1	24.08	H
ATOM	4640	HB2	GLN C	143	−0.614	57.098	−7.732	1	22.76	H
ATOM	4641	HB3	GLN C	143	−1.906	56.561	−8.482	1	22.76	H
ATOM	4642	HG2	GLN C	143	2.094	58.54	−9.651	1	21.52	H
ATOM	4643	HG3	GLN C	143	−0.877	59.162	−8.84	1	21.52	H
ATOM	4644	HE21	GLN C	143	−0.302	57.225	−12.079	1	20.49	H
ATOM	4645	HE22	GLN C	143	−1.653	57.609	−11.584	1	20.49	H
ATOM	4646	N	ASP C	144	−2.77	57.395	−4.639	1	22.78	N
ATOM	4647	CA	ASP C	144	−2.791	56.572	−3.438	1	23.8	C
ATOM	4648	C	ASP C	144	−3.893	55.512	−3.492	1	19.24	C
ATOM	4649	O	ASP C	144	−3.854	54.538	−2.74	1	21.24	O
ATOM	4650	CB	ASP C	144	−2.949	57.449	−2.188	1	24.8	C
ATOM	4651	CG	ASP C	144	−4.205	58.296	−2.215	1	24.61	C
ATOM	4652	OD1	ASP C	144	−4.881	58.345	−3.264	1	31.09	O
ATOM	4653	OD2	ASP C	144	−4.511	58.927	−1.183	1	34.04	O1−
ATOM	4654	H	ASP C	144	−2.998	58.214	−4.509	1	27.33	H
ATOM	4655	HA	ASP C	144	−1.942	56.108	−3.366	1	28.56	H
ATOM	4656	HB2	ASP C	144	−2.991	56.878	−1.405	1	29.76	H
ATOM	4657	HB3	ASP C	144	−2.188	58.046	−2.123	1	29.76	H
ATOM	4658	N	LEU C	145	−4.864	55.678	−4.386	1	18.41	N
ATOM	4659	CA	LEU C	145	−5.892	54.652	−4.544	1	19.62	C
ATOM	4660	C	LEU C	145	−5.274	53.321	−4.976	1	20.78	C
ATOM	4661	O	LEU C	145	−5.893	52.27	−4.826	1	14.96	O
ATOM	4662	CB	LEU C	145	−6.968	55.078	−5.553	1	19.66	C
ATOM	4663	CG	LEU C	145	−6.615	55.709	−6.908	1	27.1	C
ATOM	4664	CD1	LEU C	145	−5.336	55.184	−7.518	1	25.7	C
ATOM	4665	CD2	LEU C	145	−7.776	55.498	−7.879	1	21.56	C
ATOM	4666	H	LEU C	145	−4.95	56.36	−4.903	1	22.09	H
ATOM	4667	HA	LEU C	145	−6.328	54.513	−3.689	1	23.55	H
ATOM	4668	HB2	LEU C	145	−7.493	54.288	−5.756	1	23.59	H
ATOM	4669	HB3	LEU C	145	−7.54	55.718	−5.102	1	23.59	H
ATOM	4670	HG	LEU C	145	−6.508	56.665	−6.784	1	32.52	H
ATOM	4671	HD11	LEU C	145	−5.185	55.63	−8.366	1	30.83	H
ATOM	4672	HD12	LEU C	145	−4.6	55.366	−6.913	1	30.83	H
ATOM	4673	HD13	LEU C	145	−5.422	54.228	−7.657	1	30.83	H
ATOM	4674	HD21	LEU C	145	−7.55	55.898	8.734	1	25.87	H
ATOM	4675	HD22	LEU C	145	−7.927	54.547	−7.989	1	25.87	H
ATOM	4676	HD23	LEU C	145	−8.571	55.92	−7.517	1	25.87	H
ATOM	4677	N	LEU C	146	−4.048	53.365	−5.494	1	16.14	N
ATOM	4678	CA	LEU C	146	−3.384	52.158	−5.983	1	16.03	C
ATOM	4679	C	LEU C	146	−2.981	51.231	−4.84	1	17.57	C
ATOM	4680	O	LEU C	146	−2.655	50.065	−5.067	1	16.74	O
ATOM	4681	CB	LEU C	146	−2.154	52.524	−6.821	1	17.95	C
ATOM	4682	CG	LEU C	146	−2.41	53.275	−8.132	1	15.53	C
ATOM	4683	CD1	LEU C	146	−1.089	53.618	−8.817	1	16.96	C
ATOM	4684	CD2	LEU C	146	−3.292	52.46	9.064	1	19.12	C
ATOM	4685	H	LEU C	146	−3.579	54.081	−5.574	1	19.36	H
ATOM	4686	HA	LEU C	146	−3.999	51.673	−6.555	1	19.23	H
ATOM	4687	HB2	LEU C	146	−1.575	53.083	−6.28	1	21.54	H
ATOM	4688	HB3	LEU C	146	−1.688	51.704	−7.048	1	21.54	H
ATOM	4689	HG	LEU C	146	−2.87	54.106	−7.935	1	18.63	H
ATOM	4690	HD11	LEU C	146	−1.276	54.092	−9.642	1	20.36	H
ATOM	4691	HD12	LEU C	146	−0.564	54.179	−8.225	1	20.36	H
ATOM	4692	HD13	LEU C	146	−0.61	52.797	−9.007	1	20.36	H
ATOM	4693	HD21	LEU C	146	−3.435	52.962	−9.882	1	22.95	H
ATOM	4694	HD22	LEU C	146	−2.85	51.621	−9.264	1	22.95	H
ATOM	4695	HD23	LEU C	146	−4.142	52.291	−8.627	1	22.95	H
ATOM	4696	N	LYS C	147	−3.014	51.744	−3.613	1	19.33	N
ATOM	4697	CA	LYS C	147	−2.75	50.925	−2.433	1	19.87	C
ATOM	4698	C	LYS C	147	−3.839	49.877	−2.192	1	17.73	C
ATOM	4699	O	LYS C	147	−3.603	48.867	−1.526	1	19.26	O
ATOM	4700	CB	LYS C	147	−2.628	51.807	−1.188	1	23.96	C
ATOM	4701	CG	LYS C	147	−1.4	52.698	−1.163	1	34.05	C
ATOM	4702	CD	LYS C	147	−1.286	53.467	0.152	1	43.75	C
ATOM	4703	CE	LYS C	147	−2.464	54.413	0.354	1	52.91	C
ATOM	4704	NZ	LYS C	147	−2.213	55.423	1.423	1	63.31	N1+
ATOM	4705	H	LYS C	147	−3.187	52.568	−3.436	1	23.19	H
ATOM	4706	HA	LYS C	147	−1.908	50.459	−2.555	1	23.84	H
ATOM	4707	HB2	LYS C	147	−3.409	52.38	−1.136	1	28.75	H
ATOM	4708	HB3	LYS C	147	−2.592	51.234	−0.405	1	28.75	H
ATOM	4709	HG2	LYS C	147	−0.606	52.15	−1.263	1	40.86	H
ATOM	4710	HG3	LYS C	147	−1.458	53.341	−1.886	1	40.86	H
ATOM	4711	HD2	LYS C	147	−1.272	52.838	0.89	1	52.5	H
ATOM	4712	HD3	LYS C	147	−0.472	53.994	0.145	1	52.5	H
ATOM	4713	HE2	LYS C	147	−2.634	54.888	−0.474	1	63.49	H
ATOM	4714	HE3	LYS C	147	−3.245	53.896	0.607	1	63.49	H
ATOM	4715	HZ1	LYS C	147	−2.921	55.955	1.511	1	75.97	H
ATOM	4716	HZ2	LYS C	147	−2.06	55.014	2.198	1	75.97	H
ATOM	4717	HZ3	LYS C	147	−1.504	55.918	1.213	1	75.97	H
ATOM	4718	N	LEU C	148	−5.028	50.122	−2.732	1	15.82	N
ATOM	4719	CA	LEU C	148	−6.21	49.333	−2.387	1	18.04	C
ATOM	4720	C	LEU C	148	−6.593	48.304	−3.45	1	18.6	C
ATOM	4721	O	LEU C	148	−7.686	47.744	−3.405	1	15.31	O
ATOM	4722	CB	LEU C	148	−7.395	50.269	−2.151	1	23.06	C
ATOM	4723	CG	LEU C		148	−7.13	51.452	−1.217	1	32.15	C
ATOM	4724	CD1	LEU C	148	−8.009	52.619	−1.612	1	32.37	C
ATOM	4725	CD2	LEU C	148	−7.363	51.056	0.236	1	30.03	C
ATOM	4726	H	LEU C		148	−5.179	50.745	−3.306	1	18.98	H
ATOM	4727	HA	LEU C	148	−6.038	48.856	−1.56	1	21.65	H
ATOM	4728	HB2	LEU C	148	−7.674	50.632	−3.007	1	27.68	H
ATOM	4729	HB3	LEU C	148	−8.122	49.753	−1.768	1	27.68	H
ATOM	4730	HG	LEU C		148	−6.204	51.727	−1.308	1	38.58	H
ATOM	4731	HD11	LEU C	148	−7.833	53.363	−1.015	1	38.84	H
ATOM	4732	HD12	LEU C	148	−7.804	52.873	−2.526	1	38.84	H
ATOM	4733	HD13	LEU C	148	−8.939	52.351	−1.544	1	38.84	H
ATOM	4734	HD21	LEU C	148	−7.188	51.822	0.804	1	36.04	H
ATOM	4735	HD22	LEU C	148	−8.284	50.77	0.341	1	36.04	H
ATOM	4736	HD23	LEU C	148	−6.763	50.329	0.466	1	36.04	H
ATOM	4737	N	VAL C		149	−5.697	48.054	−4.398	1	16.71	N
ATOM	4738	CA	VAL C	149	−6.011	47.21	−5.548	1	14.87	C
ATOM	4739	C	VAL C	149	5.503	45.783	−5.38	1	14.53	C
ATOM	4740	O	VAL C	149	−4.311	45.568	−5.166	1	16.23	O
ATOM	4741	CB	VAL C	149	−5.409	47.803	−6.833	1	18.92	C
ATOM	4742	CG1	VAL C	149	−5.723	46.926	−8.036	1	20.42	C
ATOM	4743	CG2	VAL C	149	−5.93	49.222	−7.054	1	20.99	C
ATOM	4744	H	VAL C		149	−4.894	48.363	−4.399	1	20.06	H
ATOM	4745	HA	VAL C	149	−6.975	47.174	−5.658	1	17.84	H
ATOM	4746	HB	VAL C	149	−4.445	47.849	6.738	1	22.71	H
ATOM	4747	HG11	VAL C	149	−5.33	47.326	−8.828	1	24.51	H
ATOM	4748	HG12	VAL C	149	−5.347	46.044	−7.89	1	24.51	H
ATOM	4749	HG13	VAL C	149	−6.685	46.864	−8.139	1	24.51	H
ATOM	4750	HG21	VAL C	149	−5.539	49.577	−7.868	1	25.18	H
ATOM	4751	HG22	VAL C	149	−6.896	49.194	−7.136	1	25.18	H
ATOM	4752	HG23	VAL C	149	−5.677	49.772	−6.297	1	25.18	H
ATOM	4753	N	LYS C	150	−6.408	44.816	−5.5	1	13.93	N
ATOM	4754	CA	LYS C	150	−6.044	43.402	−5.45	1	18.06	C
ATOM	4755	C	LYS C	150	−5.531	42.912	−6.797	1	15.46	C
ATOM	4756	O	LYS C	150	−5.715	43.57	−7.819	1	15.34	O
ATOM	4757	CB	LYS C	150	−7.238	42.538	−5.03	1	16.72	C
ATOM	4758	CG	LYS C	150	−7.584	42.607	−3.553	1	17.69	C
ATOM	4759	CD	LYS C	150	−8.705	41.641	−3.194	1	15.55	C
ATOM	4760	CE	LYS C	150	−8.218	40.202	−3.082	1	17.69	C
ATOM	4761	NZ	LYS C	150	−7.374	39.972	−1.871	1	15.2	N1+
ATOM	4762	H	LYS C	150	−7.249	44.953	−5.613	1	16.72	H
ATOM	4763	HA	LYS C	150	−5.338	43.279	−4.796	1	21.68	H
ATOM	4764	HB2	LYS C	150	−8.019	42.826	−5.528	1	20.06	H
ATOM	4765	HB3	LYS C	150	−7.04	41.612	−5.241	1	20.06	H
ATOM	4766	HG2	LYS C	150	−6.802	42.373	−3.03	1	21.22	H
ATOM	4767	HG3	LYS C	150	−7.877	43.506	−3.335	1	21.22	H
ATOM	4768	HD2	LYS C	150	−9.084	41.898	−2.339	1	18.65	H
ATOM	4769	HD3	LYS C	150	−9.386	41.675	−3.884	1	18.65	H
ATOM	4770	HE2	LYS C	150	−8.986	39.612	−3.029	1	21.23	H
ATOM	4771	HE3	LYS C	150	−7.686	39.987	−3.864	1	21.23	H
ATOM	4772	HZ1	LYS C	150	−6.656	40.498	−1.896	1	18.24	H
ATOM	4773	HZ2	LYS C	150	−7.841	40.156	−1.136	1	18.24	H
ATOM	4774	HZ3	LYS C	150	−7.11	39.123	1.841	1	18.24	H
ATOM	4775	N	SER C	151	−4.903	41.742	−6.777	1	16.11	N
ATOM	4776	CA	SER C	151	−4.426	41.078	−7.985	1	17.4	C
ATOM	4777	C	SER C	151	−3.319	41.859	−8.69	1	14.09	C
ATOM	4778	O	SER C	151	−2.799	42.846	−8.168	1	16.03	O
ATOM	4779	CB	SER C	151	−5.585	40.834	−8.952	1	14.05	C
ATOM	4780	OG	SER C	151	−5.188	39.954	−9.988	1	14.91	O
ATOM	4781	H	SER C	151	−4.736	41.302	−6.057	1	19.33	H
ATOM	4782	HA	SER C	151	−4.063	40.213	−7.739	1	20.89	H
ATOM	4783	HB2	SER C	151	−6.325	40.438	−8.467	1	16.86	H
ATOM	4784	HB3	SER C	151	5.856	41.679	−9.342	1	16.86	H
ATOM	4785	HG	SER C	151	−5.828	39.824	−10.515	1	17.89	H
ATOM	4786	N	TYR C	152	−2.961	41.385	−9.877	1	12.6	N
ATOM	4787	CA	TYR C	152	−1.828	41.905	−10.624	1	11.73	C
ATOM	4788	C	TYR C	152	−2.312	42.429	−11.968	1	17.09	C
ATOM	4789	O	TYR C	152	−3.22	41.852	−12.575	1	15.23	O
ATOM	4790	CB	TYR C	152	−0.77	40.814	−10.824	1	14.94	C
ATOM	4791	CG	TYR C	152	−0.394	40.065	−9.562	1	13.45	C
ATOM	4792	CD1	TYR C	152	−0.119	40.743	−8.383	1	17.53	C
ATOM	4793	CD2	TYR C	152	−0.317	38.678	−9.552	1	13.04	C
ATOM	4794	CE1	TYR C	152	0.229	40.064	−7.232	1	15.99	C
ATOM	4795	CE2	TYR C	152	0.031	37.989	8.407	1	17.54	C
ATOM	4796	CZ	TYR C	152	0.303	38.688	−7.246	1	17.26	C
ATOM	4797	OH	TYR C	152	0.65	38.009	−6.097	1	14.46	O
ATOM	4798	H	TYR C	152	−3.371	40.745	−10.28	1	15.12	H
ATOM	4799	HA	TYR C	152	−1.425	42.639	−10.134	1	14.07	H
ATOM	4800	HB2	TYR C	152	−1.11	40.166	−11.461	1	17.93	H
ATOM	4801	HB3	TYR C	152	0.036	41.224	−11.174	1	17.93	H
ATOM	4802	HD1	TYR C	152	−0.165	41.672	−8.369	1	21.04	H
ATOM	4803	HD2	TYR C	152	−0.496	38.205	−10.333	1	15.65	H
ATOM	4804	HE1	TYR C	152	0.412	40.533	−6.45	1	19.18	H
ATOM	4805	HE2	TYR C	152	0.08	37.06	−8.416	1	21.05	H
ATOM	4806	HH	TYR C	152	0.657	37.182	−6.243	1	17.36	H
ATOM	4807	N	HIS C	153	−1.711	43.521	−12.428	1	11.85	N
ATOM	4808	CA	HIS C	153	−2.185	44.203	−13.628	1	13.69	C
ATOM	4809	C	HIS C	153	−1.038	44.802	−14.415	1	13.1	C
ATOM	4810	O	HIS C	153	−0.106	45.358	−13.836	1	13.18	O
ATOM	4811	CB	HIS C	153	−3.182	45.302	−13.254	1	12.79	C
ATOM	4812	CG	HIS C	153	−4.22	44.86	−12.274	1	15.44	C
ATOM	4813	ND1	HIS C	153	−5.444	44.357	−12.661	1	13.49	N
ATOM	4814	CD2	HIS C	153	−4.21	44.83	−10.92	1	15.97	C
ATOM	4815	CE1	HIS C	153	−6.146	44.043	−11.587	1	16.56	C
ATOM	4816	NE2	HIS C	153	−5.419	44.317	−10.518	1	16.62	N
ATOM	4817	H	HIS C	153	−1.025	43.888	−12.063	1	14.22	H
ATOM	4818	HA	HIS C	153	−2.641	43.563	−14.198	1	16.43	H
ATOM	4819	HB2	HIS C	153	−2.697	46.043	−12.859	1	15.35	H
ATOM	4820	HB3	HIS C	153	−3.638	45.598	−14.057	1	15.35	H
ATOM	4821	HD1	HIS C	153	−5.71	44.265	−13.474	1	16.19	H
ATOM	4822	HD2	HIS C	153	−3.515	45.104	−10.366	1	19.16	H
ATOM	4823	HE1	HIS C	153	−7.005	43.687	−11.584	1	19.87	H
ATOM	4824	HE2	HIS C	153	−5.665	44.199	−9.702	1	19.95	H
ATOM	4825	N	TRP C	154	−1.104	44.682	−15.738	1	15.58	N
ATOM	4826	CA	TRP C	154	−0.104	45.295	−16.598	1	15.13	C
ATOM	4827	C	TRP C	154	−0.118	46.805	−16.411	1	15.13	C
ATOM	4828	O	TRP C	154	−1.175	47.43	−16.468	1	13.3	O
ATOM	4829	CB	TRP C	154	−0.353	44.977	−18.078	1	15.45	C
ATOM	4830	CG	TRP C	154	0.036	43.598	−18.543	1	17.21	C
ATOM	4831	CD1	TRP C	154	−0.751	42.717	−19.229	1	18.69	C
ATOM	4832	CD2	TRP C	154	1.31	42.957	−18.385	1	17.34	C
ATOM	4833	NE1	TRP C	154	−0.049	41.567	−19.506	1	16.22	N
ATOM	4834	CE2	TRP C	154	1.217	41.687	−18.995	1	17.13	C
ATOM	4835	CE3	TRP C	154	2.518	43.329	−17.783	1	15.92	C
ATOM	4836	CZ2	TRP C	154	2.283	40.79	−19.019	1	16.67	C
ATOM	4837	CZ3	TRP C	154	3.576	42.435	−17.809	1	13.5	C
ATOM	4838	CH2	TRP C	154	3.451	41.182	−18.422	1	14.99	C
ATOM	4839	H	TRP C	154	−1.718	44.251	−16.159	1	18.7	H
ATOM	4840	HA	TRP C	154	0.775	44.964	−16.357	1	18.16	H
ATOM	4841	HB2	TRP C	154	−1.301	45.083	−18.256	1	18.54	H
ATOM	4842	HB3	TRP C	154	0.147	45.612	−18.613	1	18.54	H
ATOM	4843	HD1	TRP C	154	−1.633	42.875	−19.48	1	22.43	H
ATOM	4844	HE1	TRP C	154	−0.357	40.881	−19.924	1	19.46	H
ATOM	4845	HE3	TRP C	154	2.608	44.16	−17.375	1	19.1	H
ATOM	4846	HZ2	TRP C	154	2.203	39.957	−19.424	1	20.01	H
ATOM	4847	HZ3	TRP C	154	4.383	42.671	−17.413	1	16.2	H
ATOM	4848	HH2	TRP C	154	4.179	40.603	−18.422	1	17.99	H
ATOM	4849	N	MET C	155	1.06	47.377	−16.184	1	13.13	N
ATOM	4850	CA	MET C	155	1.247	48.82	−16.244	1	15.17	C
ATOM	4851	C	MET C	155	2.264	49.134	−17.341	1	17.69	C
ATOM	4852	O	MET C	155	2.792	48.226	−17.983	1	15.06	O
ATOM	4853	CB	MET C	155	1.705	49.374	−14.895	1	13.1	C
ATOM	4854	CG	MET C	155	2.991	48.776	−14.369	1	12.38	C
ATOM	4855	SD	MET C	155	3.439	49.474	−12.769	1	15.66	S
ATOM	4856	CE	MET C	155	4.634	48.273	−12.207	1	16.77	C
ATOM	4857	H	MET C	155	1.776	46.943	−15.989	1	15.75	H
ATOM	4858	HA	MET C	155	0.402	49.239	−16.468	1	18.2	H
ATOM	4859	HB2	MET C	155	1.841	50.33	−14.983	1	15.72	H
ATOM	4860	HB3	MET C	155	1.012	49.202	−14.238	1	15.72	H
ATOM	4861	HG2	MET C	155	2.879	47.818	−14.262	1	14.86	H
ATOM	4862	HG3	MET C	155	3.71	48.962	−14.994	1	14.86	H
ATOM	4863	HE1	MET C	155	4.961	48.538	−11.333	1	20.13	H
ATOM	4864	HE2	MET C	155	4.205	47.404	−12.15	1	20.13	H
ATOM	4865	HE3	MET C	155	5.369	48.239	−12.839	1	20.13	H
ATOM	4866	N	GLY C	156	2.542	50.415	−17.549	1	15.94	N
ATOM	4867	CA	GLY C	156	3.297	50.843	−18.714	1	17.37	C
ATOM	4868	C	GLY C	156	4.802	50.829	−18.544	1	19.77	C
ATOM	4869	O	GLY C	156	5.513	51.512	−19.281	1	21.61	O
ATOM	4870	H	GLY C	156	2.304	51.057	−17.029	1	19.13	H
ATOM	4871	HA2	GLY C	156	3.076	50.264	−19.461	1	20.84	H
ATOM	4872	HA3	GLY C	156	3.031	51.746	−18.947	1	20.84	H
ATOM	4873	N	LEU C	157	5.289	50.047	−17.585	1	18.34	N
ATOM	4874	CA	LEU C	157	6.714	50.015	−17.271	1	17.73	C
ATOM	4875	C	LEU C	157	7.415	48.89	−18.029	1	18.37	C
ATOM	4876	O	LEU C	157	7.014	47.726	−17.935	1	16.44	O
ATOM	4877	CB	LEU C	157	6.922	49.845	−15.762	1	19.33	C
ATOM	4878	CG	LEU C	157	8.315	50.182	−15.225	1	17.68	C
ATOM	4879	CD1	LEU C	157	8.587	51.676	−15.326	1	18.67	C
ATOM	4880	CD2	LEU C	157	8.458	49.706	−13.788	1	20.64	C
ATOM	4881	H	LEU C	157	4.812	49.522	−17.099	1	22.01	H
ATOM	4882	HA	LEU C	157	7.117	50.856	−17.538	1	21.28	H
ATOM	4883	HB2	LEU C	157	6.29	50.418	−15.302	1	23.19	H
ATOM	4884	HB3	LEU C	157	6.742	48.919	−15.534	1	23.19	H
ATOM	4885	HG	LEU C	157	8.979	49.72	−15.76	1	21.22	H
ATOM	4886	HD11	LEU C	157	9.474	51.859	−14.979	1	22.41	H
ATOM	4887	HD12	LEU C	157	8.533	51.944	−16.257	1	22.41	H
ATOM	4888	HD13	LEU C	157	7.922	52.153	−14.805	1	22.41	H
ATOM	4889	HD21	LEU C	157	9.346	49.93	−13.469	1	24.77	H
ATOM	4890	HD22	LEU C	157	7.788	50.147	−13.242	1	24.77	H
ATOM	4891	HD23	LEU C	157	8.327	48.745	−13.759	1	24.77	H
ATOM	4892	N	VAL C	158	8.462	49.247	−18.774	1	19.08	N
ATOM	4893	CA	VAL C	158	9.199	48.292	−19.595	1	18.04	C
ATOM	4894	C	VAL C	158	10.704	48.381	−19.349	1	20.45	C
ATOM	4895	O	VAL C	158	11.209	49.396	−18.873	1	18.61	O
ATOM	4896	CB	VAL C	158	8.931	48.512	−21.093	1	17.89	C
ATOM	4897	CG1	VAL C	158	7.446	48.311	−21.402	1	18.67	C
ATOM	4898	CG2	VAL C	158	9.398	49.897	−21.522	1	16.63	C
ATOM	4899	H	VAL C	158	8.768	50.049	−18.819	1	22.89	H
ATOM	4900	HA	VAL C	158	8.911	47.394	−19.369	1	21.65	H
ATOM	4901	HB	VAL C	158	9.433	47.857	−21.602	1	21.47	H
ATOM	4902	HG11	VAL C	158	7.299	48.454	−22.35	1	22.4	H
ATOM	4903	HG12	VAL C	158	7.194	47.405	−21.161	1	22.4	H
ATOM	4904	HG13	VAL C	158	6.927	48.947	−20.887	1	22.4	H
ATOM	4905	HG21	VAL C	158	9.218	50.011	−22.469	1	19.96	H
ATOM	4906	HG22	VAL C	158	8.916	50.565	−21.01	1	19.96	H
ATOM	4907	HG23	VAL C	158	10.35	49.975	−21.354	1	19.96	H
ATOM	4908	N	HIS C	159	11.405	47.314	−19.716	1	16.25	N
ATOM	4909	CA	HIS C	159	12.812	47.135	−19.375	1	21	C
ATOM	4910	C	HIS C	159	13.698	47.078	−20.616	1	21.62	C
ATOM	4911	O	HIS C	159	13.47	46.273	−21.516	1	19.38	O
ATOM	4912	CB	HIS C	159	12.968	45.855	−18.552	1	25.11	C
ATOM	4913	CG	HIS C	159	14.385	45.484	−18.249	1	23.93	C
ATOM	4914	ND1	HIS C	159	15.041	44.462	−18.901	1	30.14	N
ATOM	4915	CD2	HIS C	159	15.265	45.983	−17.348	1	28.59	C
ATOM	4916	CE1	HIS C	159	16.269	44.354	−18.423	1	30.59	C
ATOM	4917	NE2	HIS C	159	16.43	45.265	−17.479	1	31.14	N
ATOM	4918	H	HIS C	159	11.079	46.663	−20.174	1	19.5	H
ATOM	4919	HA	HIS C	159	13.104	47.882	−18.83	1	25.2	H
ATOM	4920	HB2	HIS C	159	12.507	45.971	−17.706	1	30.13	H
ATOM	4921	HB3	HIS C	159	12.57	45.119	−19.043	1	30.13	H
ATOM	4922	HD1	HIS C	159	14.706	43.974	−19.525	1	36.16	H
ATOM	4923	HD2	HIS C	159	15.112	46.683	−16.756	1	34.31	H
ATOM	4924	HE1	HIS C	159	16.91	43.742	−18.703	1	36.71	H
ATOM	4925	HE2	HIS C	159	17.147	45.39	−17.022	1	37.37	H
ATOM	4926	N	ILE C	160	14.703	47.947	−20.656	1	25.17	N
ATOM	4927	CA	ILE C	160	15.714	47.923	−21.708	1	25.24	C
ATOM	4928	C	ILE C	160	16.835	46.958	−21.317	1	32.27	C
ATOM	4929	O	ILE C	160	17.581	47.241	−20.379	1	31.75	O
ATOM	4930	CB	ILE C	160	16.31	49.328	−21.947	1	29.66	C
ATOM	4931	CG1	ILE C	160	15.219	50.296	−22.407	1	26.24	C
ATOM	4932	CG2	ILE C	160	17.433	49.264	−22.976	1	33.94	C
ATOM	4933	CD1	ILE C	160	15.673	51.741	−22.507	1	35.2	C
ATOM	4934	H	ILE C	160	14.822	48.571	−20.076	1	30.21	H
ATOM	4935	HA	ILE C	160	15.314	47.613	−22.535	1	30.29	H
ATOM	4936	HB	ILE C	160	16.677	49.653	−21.11	1	35.59	H
ATOM	4937	HG12	ILE C	160	14.91	50.022	−23.284	1	31.49	H
ATOM	4938	HG13	ILE C	160	14.485	50.26	−21.774	1	31.49	H
ATOM	4939	HG21	ILE C	160	17.79	50.156	−23.108	1	40.72	H
ATOM	4940	HG22	ILE C	160	18.129	48.674	−22.646	1	40.72	H
ATOM	4941	HG23	ILE C	160	17.077	48.923	−23.811	1	40.72	H
ATOM	4942	HD11	ILE C	160	14.926	52.285	−22.803	1	42.25	H
ATOM	4943	HD12	ILE C	160	15.974	52.038	−21.635	1	42.25	H
ATOM	4944	HD13	ILE C	160	16.4	51.799	−23.147	1	42.25	H
ATOM	4945	N	PRO C	161	16.965	45.817	−22.025	1	32.29	N
ATOM	4946	CA	PRO C	161	18.018	44.864	−21.642	1	33.49	C
ATOM	4947	C	PRO C	161	19.426	45.439	−21.793	1	38.43	C
ATOM	4948	O	PRO C	161	20.344	45.006	−21.093	1	39.19	O
ATOM	4949	CB	PRO C	161	17.81	43.692	−22.612	1	34.26	C
ATOM	4950	CG	PRO C	161	16.429	43.848	−23.134	1	31.11	C
ATOM	4951	CD	PRO C	161	16.174	45.321	−23.164	1	27.41	C
ATOM	4952	HA	PRO C	161	17.887	44.559	−20.731	1	40.18	H
ATOM	4953	HB2	PRO C	161	18.456	43.747	−23.333	1	41.12	H
ATOM	4954	HB3	PRO C	161	17.902	42.853	−22.134	1	41.12	H
ATOM	4955	HG2	PRO C	161	16.374	43.474	−24.028	1	37.33	H
ATOM	4956	HG3	PRO C	161	15.804	43.405	−22.539	1	37.33	H
ATOM	4957	HD2	PRO C	161	16.497	45.705	−23.994	1	32.89	H
ATOM	4958	HD3	PRO C	161	15.231	45.505	−23.028	1	32.89	H
ATOM	4959	N	THR C	162	19.577	46.399	−22.701	1	41.08	N
ATOM	4960	CA	THR C	162	20.863	47.035	−22.974	1	43.65	C
ATOM	4961	C	THR C	162	21.495	47.605	−21.709	1	48.57	C
ATOM	4962	O	THR C	162	22.589	47.196	−21.318	1	52.38	O
ATOM	4963	CB	THR C	162	20.704	48.164	−24.03	1	41.19	C
ATOM	4964	OG1	THR C	162	20.643	47.588	−25.339	1	51.79	O
ATOM	4965	CG2	THR C	162	21.861	49.168	−23.983	1	50.32	C
ATOM	4966	H	THR C	162	18.934	46.707	−23.182	1	49.29	H
ATOM	4967	HA	THR C	162	21.47	46.371	−23.337	1	52.38	H
ATOM	4968	HB	THR C	162	19.88	48.646	−23.857	1	49.42	H
ATOM	4969	HG1	THR C	162	19.988	47.065	−25.393	1	62.14	H
ATOM	4970	HG21	THR C	162	21.73	49.857	−24.653	1	60.38	H
ATOM	4971	HG22	THR C	162	21.904	49.584	−23.107	1	60.38	H
ATOM	4972	HG23	THR C	162	22.701	48.714	−24.157	1	60.38	H
ATOM	4973	N	ASN C	163	20.799	48.544	−21.075	1	46.77	N
ATOM	4974	CA	ASN C	163	21.34	49.264	−19.928	1	44.73	C
ATOM	4975	C	ASN C	163	20.59	48.965	−18.63	1	46.38	C
ATOM	4976	O	ASN C	163	20.716	49.698	−17.648	1	47.39	O
ATOM	4977	CB	ASN C	163	21.324	50.768	−20.213	1	48.3	C
ATOM	4978	CG	ASN C	163	19.972	51.258	−20.685	1	47.25	C
ATOM	4979	OD1	ASN C	163	18.934	50.711	−20.313	1	46.02	O
ATOM	4980	ND2	ASN C	163	19.978	52.292	−21.52	1	46.65	N
ATOM	4981	H	ASN C	163	20.003	48.784	−21.292	1	56.13	H
ATOM	4982	HA	ASN C	163	22.264	48.998	−19.802	1	53.68	H
ATOM	4983	HB2	ASN C	163	21.55	51.246	−19.399	1	57.96	H
ATOM	4984	HB3	ASN C	163	21.974	50.965	−20.905	1	57.96	H
ATOM	4985	HD21	ASN C	163	19.236	52.608	−21.817	1	55.98	H
ATOM	4986	HD22	ASN C	163	20.724	52.645	−21.762	1	55.98	H
ATOM	4987	N	GLY C	164	19.813	47.885	−18.633	1	43.17	N
ATOM	4988	CA	GLY C	164	19.118	47.429	−17.441	1	38.67	C
ATOM	4989	C	GLY C	164	18.202	48.466	−16.815	1	39.65	C
ATOM	4990	O	GLY C	164	17.958	48.435	−15.609	1	42.49	O
ATOM	4991	H	GLY C	164	19.673	47.394	−19.326	1	51.8	H
ATOM	4992	HA2	GLY C	164	18.584	46.651	−17.664	1	46.4	H
ATOM	4993	HA3	GLY C	164	19.772	47.165	−16.775	1	46.4	H
ATOM	4994	N	SER C	165	17.686	49.376	−17.636	1	34.82	N
ATOM	4995	CA	SER C	165	16.856	50.474	−17.153	1	32.2	C
ATOM	4996	C	SER C	165	15.364	50.169	−17.287	1	27.87	C
ATOM	4997	O	SER C	165	14.943	49.486	−18.223	1	25.68	O
ATOM	4998	CB	SER C	165	17.193	51.756	−17.917	1	38.18	C
ATOM	4999	OG	SER C	165	16.391	52.837	−17.475	1	43.62	O
ATOM	5000	H	SER C	165	17.803	49.378	−18.488	1	41.79	H
ATOM	5001	HA	SER C	165	17.048	50.625	−16.214	1	38.64	H
ATOM	5002	HB2	SER C	165	18.126	51.976	−17.769	1	45.81	H
ATOM	5003	HB3	SER C	165	17.032	51.611	−18.863	1	45.81	H
ATOM	5004	HG	SER C	165	16.586	53.533	−17.903	1	52.34	H
ATOM	5005	N	TRP C	166	14.579	50.679	−16.34	1	31.94	N
ATOM	5006	CA	TRP C	166	13.119	50.583	−16.387	1	23.07	C
ATOM	5007	C	TRP C	166	12.515	51.944	−16.699	1	27.85	C
ATOM	5008	O	TRP C	166	12.805	52.927	−16.018	1	29.97	O
ATOM	5009	CB	TRP C	166	12.561	50.059	−15.063	1	22.45	C
ATOM	5010	CG	TRP C	166	12.817	48.608	−14.846	1	20.87	C
ATOM	5011	CD1	TRP C	166	13.887	48.054	−14.214	1	28.32	C
ATOM	5012	CD2	TRP C	166	11.989	47.519	−15.267	1	20.19	C
ATOM	5013	NE1	TRP C	166	13.779	46.685	−14.212	1	29.81	N
ATOM	5014	CE2	TRP C	166	12.622	46.331	−14.853	1	21.03	C
ATOM	5015	CE3	TRP C	166	10.773	47.434	−15.951	1	18.26	C
ATOM	5016	CZ2	TRP C	166	12.082	45.074	−15.1	1	20.42	C
ATOM	5017	CZ3	TRP C	166	10.238	46.186	−16.198	1	19.14	C
ATOM	5018	CH2	TRP C	166	10.89	45.02	−15.772	1	22.75	C
ATOM	5019	H	TRP C	166	14.873	51.093	−15.646	1	38.33	H
ATOM	5020	HA	TRP C	166	12.861	49.968	−17.091	1	27.68	H
ATOM	5021	HB2	TRP C	166	12.974	50.547	−14.334	1	26.94	H
ATOM	5022	HB3	TRP C	166	11.601	50.197	−15.051	1	26.94	H
ATOM	5023	HD1	TRP C	166	14.591	48.532	−13.838	1	33.98	H
ATOM	5024	HE1	TRP C	166	14.345	46.139	−13.865	1	35.77	H
ATOM	5025	HE3	TRP C	166	10.335	48.203	−16.237	1	21.91	H
ATOM	5026	HZ2	TRP C	166	12.513	44.299	−14.818	1	24.5	H
ATOM	5027	HZ3	TRP C	166	9.429	46.117	−16.653	1	22.96	H
ATOM	5028	HH2	TRP C	166	10.506	44.192	−15.952	1	27.3	H
ATOM	5029	N	GLN C	167	11.676	52.003	−17.727	1	22.33	N
ATOM	5030	CA	GLN C	167	11.066	53.265	−18.126	1	24.92	C
ATOM	5031	C	GLN C	167	9.614	53.084	−18.554	1	20.54	C
ATOM	5032	O	GLN C	167	9.185	51.984	−18.912	1	18.82	O
ATOM	5033	CB	GLN C	167	11.872	53.904	−19.257	1	26.21	C
ATOM	5034	CG	GLN C	167	11.91	53.089	−20.54	1	31.52	C
ATOM	5035	CD	GLN C	167	12.781	53.73	−21.61	1	33.46	C
ATOM	5036	OE1	GLN C	167	13.768	54.399	−21.306	1	35.78	O
ATOM	5037	NE2	GLN C	167	12.412	53.532	−22.87	1	34.85	N
ATOM	5038	H	GLN C	167	11.444	51.33	−18.209	1	26.8	H
ATOM	5039	HA	GLN C	167	11.08	53.873	−17.37	1	29.9	H
ATOM	5040	HB2	GLN C	167	11.482	54.767	−19.467	1	31.45	H
ATOM	5041	HB3	GLN C	167	12.787	54.024	−18.958	1	31.45	H
ATOM	5042	HG2	GLN C	167	12.269	52.209	−20.347	1	37.82	H
ATOM	5043	HG3	GLN C	167	11.009	53.011	−20.892	1	37.82	H
ATOM	5044	HE21	GLN C	167	12.872	53.873	−23.511	1	41.82	H
ATOM	5045	HE22	GLN C	167	11.713	53.062	−23.044	1	41.82	H
ATOM	5046	N	TRP C	168	8.865	54.18	−18.504	1	19.48	N
ATOM	5047	CA	TRP C	168	7.471	54.186	−18.926	1	24.91	C
ATOM	5048	C	TRP C	168	7.401	54.322	−20.439	1	28.19	C
ATOM	5049	O	TRP C	168	B.39	54.684	−21.077	1	29.68	O
ATOM	5050	CB	TRP C	168	6.715	55.32	−18.236	1	22.9	C
ATOM	5051	CG	TRP C	168	6.806	55.241	−16.746	1	18.59	C
ATOM	5052	CD1	TRP C	168	7.589	56.003	−15.932	1	20.28	C
ATOM	5053	CD2	TRP C	168	6.101	54.331	−15.89	1	18.57	C
ATOM	5054	NE1	TRP C	168	7.41	55.631	−14.62	1	19.79	N
ATOM	5055	CE2	TRP C	168	6.501	54.607	−14.568	1	18.17	C
ATOM	5056	CE3	TRP C	168	5.168	53.313	−16.114	1	19.34	C
ATOM	5057	CZ2	TRP C	168	6	53.903	−13.474	1	19.51	C
ATOM	5058	CZ3	TRP C	168	4.672	52.614	−15.028	1	18.19	C
ATOM	5059	CH2	TRP C	168	5.09	52.912	−13.724	1	17.53	C
ATOM	5060	H	TRP C	168	9.146	54.943	−18.225	1	23.37	H
ATOM	5061	HA	TRP C	168	7.056	53.346	−18.676	1	29.89	H
ATOM	5062	HB2	TRP C	168	7.091	56.169	−18.516	1	27.48	H
ATOM	5063	HB3	TRP C	168	5.778	55.272	−18.483	1	27.48	H
ATOM	5064	HD1	TRP C	168	8.158	56.679	−16.222	1	24.34	H
ATOM	5065	HE1	TRP C	168	7.804	55.985	−13.942	1	23.74	H
ATOM	5066	HE3	TRP C	168	4.886	53.11	−16.977	1	23.2	H
ATOM	5067	HZ2	TRP C	168	6.276	54.098	−12.607	1	23.42	H
ATOM	5068	HZ3	TRP C	168	4.051	51.936	−15.166	1	21.83	H
ATOM	5069	HH2	TRP C	168	4.739	52.427	−13.013	1	21.04	H
ATOM	5070	N	GLU C	169	6.242	54.03	−21.02	1	30.7	N
ATOM	5071	CA	GLU C	169	6.122	54.022	−22.474	1	35.6	C
ATOM	5072	C	GLU C	169	6.155	55.434	−23.049	1	36.18	C
ATOM	5073	O	GLU C	169	6.337	55.608	−24.254	1	37.85	O
ATOM	5074	CB	GLU C	169	4.844	53.301	−22.91	1	39.61	C
ATOM	5075	CG	GLU C	169	3.559	53.974	−22.49	1	33.74	C
ATOM	5076	CD	GLU C	169	2.372	53.021	−22.532	1	38.01	C
ATOM	5077	OE1	GLU C	169	2.228	52.285	−23.532	1	37.73	O
ATOM	5078	OE2	GLU C	169	1.587	53.002	−21.562	1	35.4	O1−
ATOM	5079	H	GLU C	169	5.517	53.835	−20.6	1	36.84	H
ATOM	5080	HA	GLU C	169	6.876	53.536	−22.844	1	42.72	H
ATOM	5081	HB2	GLU C	169	4.84	53.24	−23.878	1	47.53	H
ATOM	5082	HB3	GLU C	169	4.847	52.41	−22.528	1	47.53	H
ATOM	5083	HG2	GLU C	169	3.653	54.299	−21.581	1	40.49	H
ATOM	5084	HG3	GLU C	169	3.375	54.712	−23.092	1	40.49	H
ATOM	5085	N	ASP C	170	5.994	56.44	−22.192	1	34.47	N
ATOM	5086	CA	ASP C	170	6.132	57.827	−22.629	1	33.57	C
ATOM	5087	C	ASP C	170	7.609	58.221	−22.703	1	33.88	C
ATOM	5088	O	ASP C	170	7.943	59.327	−23.127	1	37.21	O
ATOM	5089	CB	ASP C	170	5.363	58.777	−21.699	1	36.54	C
ATOM	5090	CG	ASP C	170	6.038	58.968	−20.348	1	37.03	C
ATOM	5091	OD1	ASP C	170	6.943	58.181	−19.995	1	34.2	O
ATOM	5092	OD2	ASP C	170	5.647	59.913	−19.628	1	37.14	O1−
ATOM	5093	H	ASP C	170	5.805	56.348	−21.358	1	41.36	H
ATOM	5094	HA	ASP C	170	5.756	57.914	−23.519	1	40.28	H
ATOM	5095	HB2	ASP C	170	5.293	59.646	−22.124	1	43.84	H
ATOM	5096	HB3	ASP C	170	4.477	58.414	−21.541	1	43.84	H
ATOM	5097	N	GLY C	171	8.484	57.311	−22.277	1	32.03	N
ATOM	5098	CA	GLY C	171	9.92	57.506	−22.382	1	35.58	C
ATOM	5099	C	GLY C	171	10.576	57.946	−21.087	1	32.1	C
ATOM	5100	O	GLY C	171	11.79	57.817	−20.924	1	32.64	O
ATOM	5101	H	GLY C	171	8.262	56.562	−21.919	1	38.44	H
ATOM	5102	HA2	GLY C	171	10.334	56.676	−22.664	1	42.69	H
ATOM	5103	HA3	GLY C	171	10.101	58.18	−23.056	1	42.69	H
ATOM	5104	N	SER C	172	9.777	58.463	−20.159	1	32.52	N
ATOM	5105	CA	SER C	172	10.301	58.957	−18.891	1	30.32	C
ATOM	5106	C	SER C	172	10.86	57.828	−18.032	1	29.58	C
ATOM	5107	O	SER C	172	10.442	56.675	−18.146	1	27.69	O
ATOM	5108	CB	SER C	172	9.213	59.703	−18.117	1	33.73	C
ATOM	5109	OG	SER C	172	8.138	58.839	−17.786	1	33.64	O
ATOM	5110	H	SER C	172	8.924	58.538	−20.24	1	39.02	H
ATOM	5111	HA	SER C	172	11.022	59.582	−19.07	1	36.38	H
ATOM	5112	HB2	SER C	172	9.595	60.058	−17.299	1	40.48	H
ATOM	5113	HB3	SER C	172	8.876	60.428	−18.666	1	40.48	H
ATOM	5114	HG	SER C	172	7.797	58.524	−18.486	1	40.37	H
ATOM	5115	N	ILE C	173	11.811	58.174	−17.17	1	28.71	N
ATOM	5116	CA	ILE C	173	12.416	57.214	−16.256	1	33.4	C
ATOM	5117	C	ILE C	173	11.462	56.904	−15.106	1	29.48	C
ATOM	5118	O	ILE C	173	10.612	57.725	−14.757	1	29.36	O
ATOM	5119	CB	ILE C	173	13.759	57.752	−15.691	1	31.94	C
ATOM	5120	CG1	ILE C	173	14.496	56.691	−14.868	1	40.78	C
ATOM	5121	CG2	ILE C	173	13.529	59	−14.843	1	39.11	C
ATOM	5122	CD1	ILE C	173	14.933	55.482	−15.661	1	47.43	C
ATOM	5123	H	ILE C	173	12.126	58.971	−17.095	1	34.45	H
ATOM	5124	HA	ILE C	173	12.596	56.388	−16.732	1	40.08	H
ATOM	5125	HB	ILE C	173	14.324	57.997	−16.44	1	38.33	H
ATOM	5126	HG12	ILE C	173	15.29	57.093	−14.482	1	48.94	H
ATOM	5127	HG13	ILE C	173	13.908	56.383	14.16	1	48.94	H
ATOM	5128	HG21	ILE C	173	14.382	59.313	−14.504	1	46.93	H
ATOM	5129	HG22	ILE C	173	13.12	59.685	−15.395	1	46.93	H
ATOM	5130	HG23	ILE C	173	12.941	58.776	−14.105	1	46.93	H
ATOM	5131	HD11	ILE C	173	14.151	55.057	−16.044	1	56.92	H
ATOM	5132	HD12	ILE C	173	15.534	55.768	−16.366	1	56.92	H
ATOM	5133	HD13	ILE C	173	15.389	54.864	−15.068	1	56.92	H
ATOM	5134	N	LEU C	174	11.589	55.712	−14.534	1	25.61	N
ATOM	5135	CA	LEU C	174	10.914	55.404	−13.281	1	23.61	C
ATOM	5136	C	LEU C	174	11.49	56.287	−12.185	1	26.93	C
ATOM	5137	O	LEU C	174	12.652	56.136	−11.819	1	26.37	O
ATOM	5138	CB	LEU C	174	11.087	53.932	−12.917	1	21.37	C
ATOM	5139	CG	LEU C		174	10.642	53.521	−11.513	1	18.27	C
ATOM	5140	CD1	LEU C	174	9.132	53.664	−11.367	1	19.7	C
ATOM	5141	CD2	LEU C		174	11.086	52.1	−11.213	1	21.64	C
ATOM	5142	H	LEU C	174	12.059	55.066	−14.851	1	30.74	H
ATOM	5143	HA	LEU C	174	9.967	55.593	−13.366	1	28.33	H
ATOM	5144	HB2	LEU C	174	10.575	53.402	−13.548	1	25.65	H
ATOM	5145	HB3	LEU C	174	12.027	53.708	−12.998	1	25.65	H
ATOM	5146	HG	LEU C		174	11.061	54.109	−10.865	1	21.92	H
ATOM	5147	HD11	LEU C	174	8.875	53.398	−10.47	1	23.64	H
ATOM	5148	HD12	LEU C	174	8.886	54.59	−11.521	1	23.64	H
ATOM	5149	HD13	LEU C	174	8.697	53.093	−12.019	1	23.64	H
ATOM	5150	HD21	LEU C	174	10.794	51.86	−10.32	1	25.97	H
ATOM	5151	HD22	LEU C	174	10.687	51.501	−11.864	1	25.97	H
ATOM	5152	HD23	LEU C	174	12.053	52.054	−11.269	1	25.97	H
ATOM	5153	N	SER C	175	10.689	57.209	−11.661	1	26.24	N
ATOM	5154	CA	SER C	175	11.166	58.084	−10.595	1	23.83	C
ATOM	5155	C	SER C	175	11.378	57.288	−9.308	1	25.15	C
ATOM	5156	O	SER C	175	10.734	56.258	−9.099	1	21.9	O
ATOM	5157	CB	SER C	175	10.187	59.234	−10.365	1	27.9	C
ATOM	5158	OG	SER C	175	10.203	60.135	−11.461	1	34.12	O
ATOM	5159	H	SER C	175	9.875	57.348	−11.901	1	31.49	H
ATOM	5160	HA	SER C	175	12.019	58.464	−10.856	1	28.6	H
ATOM	5161	HB2	SER C	175	9.293	58.873	−10.266	1	33.49	H
ATOM	5162	HB3	SER C	175	10.444	59.711	−9.56	1	33.49	H
ATOM	5163	HG	SER C	175	9.662	60.763	−11.324	1	40.94	H
ATOM	5164	N	PRO C	176	12.289	57.76	−8.44	1	23.75	N
ATOM	5165	CA	PRO C	176	12.646	57.005	−7.232	1	23.82	C
ATOM	5166	C	PRO C	176	11.56	57.003	−6.157	1	26.93	C
ATOM	5167	O	PRO C	176	10.702	57.885	−6.138	1	25	O
ATOM	5168	CB	PRO C	176	13.901	57.729	−6.726	1	30.63	C
ATOM	5169	CG	PRO C	176	13.79	59.11	−7.259	1	34.23	C
ATOM	5170	CD	PRO C	176	13.094	58.987	−8.584	1	32.51	C
ATOM	5171	HA	PRO C	176	12.873	56.091	−7.461	1	28.59	H
ATOM	5172	HB2	PRO C	176	13.907	57.735	−5.756	1	36.75	H
ATOM	5173	HB3	PRO C	176	14.694	57.29	−7.073	1	36.75	H
ATOM	5174	HG2	PRO C	176	13.266	59.652	−6.648	1	41.08	H
ATOM	5175	HG3	PRO C	176	14.676	59.486	−7.374	1	41.08	H
ATOM	5176	HD2	PRO C	176	12.518	59.753	−8.734	1	39.01	H
ATOM	5177	HD3	PRO C	176	13.742	58.884	−9.298	1	39.01	H
ATOM	5178	N	ASN C	177	11.611	56.003	−5.28	1	20.91	N
ATOM	5179	CA	ASN C	177	10.723	55.914	−4.124	1	26.58	C
ATOM	5180	C	ASN C	177	9.249	55.841	−4.507	1	27.22	C
ATOM	5181	0	ASN C	177	8.392	56.36	3.795	1	27.05	O
ATOM	5182	CB	ASN C	177	10.957	57.102	−3.188	1	28.67	C
ATOM	5183	CG	ASN C	177	12.372	57.143	−2.644	1	32.73	C
ATOM	5184	OD1	ASN C	177	12.886	56.139	−2.152	1	39.2	O
ATOM	5185	ND2	ASN C	177	13.013	58.302	−2.739	1	33.01	N
ATOM	5186	H	ASN C	177	12.166	55.348	−5.335	1	25.1	H
ATOM	5187	HA	ASN C	177	10.937	55.106	−3.632	1	31.9	H
ATOM	5188	HB2	ASN C	177	10.799	57.926	−3.676	1	34.41	H
ATOM	5189	HB3	ASN C	177	10.348	57.039	−2.436	1	34.41	H
ATOM	5190	HD21	ASN C	177	13.818	58.374	−2.444	1	39.62	H
ATOM	5191	HD22	ASN C	177	12.623	58.981	−3.095	1	39.62	H
ATOM	5192	N	LEU C	178	8.961	55.193	−5.631	1	22.55	N
ATOM	5193	CA	LEU C	178	7.586	55.018	−6.087	1	22.76	C
ATOM	5194	C	LEU C	178	7.205	53.547	−6.144	1	24.97	C
ATOM	5195	O	LEU C	178	6.143	53.162	−5.657	1	27.82	O
ATOM	5196	CB	LEU C	178	7.39	55.657	−7.461	1	21.51	C
ATOM	5197	CG	LEU C	178	7.366	57.186	−7.511	1	24.49	C
ATOM	5198	CD1	LEU C	178	7.248	57.64	−8.953	1	24.38	C
ATOM	5199	CD2	LEU C	178	6.224	57.756	−6.679	1	22.93	C
ATOM	5200	H	LEU C	178	9.549	54.842	−6.152	1	27.06	H
ATOM	5201	HA	LEU C	178	6.989	55.459	−5.463	1	27.31	H
ATOM	5202	HB2	LEU C	178	8.113	55.363	−8.037	1	25.81	H
ATOM	5203	HB3	LEU C	178	6.546	55.345	−7.822	1	25.81	H
ATOM	5204	HG	LEU C	178	8.2	57.528	−7.154	1	29.39	H
ATOM	5205	HD11	LEU C	178	7.233	58.609	−8.978	1	29.25	H
ATOM	5206	HD12	LEU C	178	8.011	57.307	−9.451	1	29.25	H
ATOM	5207	HD13	LEU C	178	6.427	57.286	−9.329	1	29.25	H
ATOM	5208	HD21	LEU C	178	6.245	58.724	−6.738	1	27.52	H
ATOM	5209	HD22	LEU C	178	5.383	57.421	−7.027	1	27.52	H
ATOM	5210	HD23	LEU C	178	6.336	57.478	−5.757	1	27.52	H
ATOM	5211	N	LEU C	179	8.075	52.732	−6.735	1	19.58	N
ATOM	5212	CA	LEU C	179	7.821	51.303	−6.896	1	17.86	C
ATOM	5213	C	LEU C	179	8.977	50.444	−6.402	1	21.63	C
ATOM	5214	O	LEU C	179	10.147	50.751	−6.648	1	22.35	O
ATOM	5215	CB	LEU C	179	7.558	50.971	8.367	1	21.35	C
ATOM	5216	CG	LEU C	179	6.29	51.513	−9.021	1	19.98	C
ATOM	5217	CD1	LEU C	179	6.291	51.174	−10.502	1	19.74	C
ATOM	5218	CD2	LEU C	179	5.044	50.954	−8.349	1	21.35	C
ATOM	5219	H	LEU C	179	8.831	52.987	−7.057	1	23.5	H
ATOM	5220	HA	LEU C	179	7.03	51.064	−6.388	1	21.44	H
ATOM	5221	HB2	LEU C	179	8.306	51.307	8.885	1	25.62	H
ATOM	5222	HB3	LEU C	179	7.526	50.005	−8.451	1	25.62	H
ATOM	5223	HG	LEU C	179	6.274	52.479	−8.932	1	23.97	H
ATOM	5224	HD11	LEU C	179	5.482	51.524	−10.906	1	23.68	H
ATOM	5225	HD12	LEU C	179	7.07	51.578	−10.917	1	23.68	H
ATOM	5226	HD13	LEU C	179	6.324	50.21	−10.605	1	23.68	H
ATOM	5227	HD21	LEU C	179	4.259	51.318	−8.788	1	25.62	H
ATOM	5228	HD22	LEU C	179	5.05	49.987	−8.429	1	25.62	H
ATOM	5229	HD23	LEU C	179	5.049	51.209	−7.414	1	25.62	H
ATOM	5230	N	THR C	180	8.639	49.362	−5.708	1	18.15	N
ATOM	5231	CA	THR C	180	9.6	48.313	−5.406	1	22.56	C
ATOM	5232	C	THR C	180	9.556	47.299	−6.548	1	20.55	C
ATOM	5233	O	THR C	180	8.552	46.607	−6.729	1	17.3	O
ATOM	5234	CB	THR C	180	9.293	47.614	−4.066	1	21.01	C
ATOM	5235	OG1	THR C	180	9.224	48.585	−3.015	1	25.27	O
ATOM	5236	CG2	THR C	180	10.368	46.594	−3.73	1	28.16	C
ATOM	5237	H	THR C	180	7.851	49.213	−5.399	1	21.78	H
ATOM	5238	HA	THR C	180	10.492	48.691	−5.362	1	27.08	H
ATOM	5239	HB	THR C	180	8.443	47.151	−4.132	1	25.22	H
ATOM	5240	HG1	THR C	180	8.616	49.142	−3.178	1	30.32	H
ATOM	5241	HG21	THR C	180	10.163	46.163	−2.886	1	33.79	H
ATOM	5242	HG22	THR C	180	10.413	45.92	−4.426	1	33.79	H
ATOM	5243	HG23	THR C	180	11.23	47.033	−3.659	1	33.79	H
ATOM	5244	N	ILE C	181	10.633	47.229	−7.325	1	19.65	N
ATOM	5245	CA	ILE C	181	10.726	46.266	−8.42	1	19.28	C
ATOM	5246	C	ILE C	181	11.226	44.924	−7.902	1	16.96	C
ATOM	5247	O	ILE C	181	12.275	44.842	−7.261	1	13.49	O
ATOM	5248	CB	ILE C	181	11.659	46.76	−9.54	1	21.11	C
ATOM	5249	CG1	ILE C	181	11.236	48.15	−10.022	1	18.12	C
ATOM	5250	CG2	ILE C	181	11.664	45.776	−10.704	1	19.77	C
ATOM	5251	CD1	ILE C	181	9.805	48.234	−10.525	1	25.78	C
ATOM	5252	H	ILE C	181	11.327	47.73	−7.24	1	23.58	H
ATOM	5253	HA	ILE C	181	9.843	46.133	−8.8	1	23.13	H
ATOM	5254	HB	ILE C	181	12.56	46.819	−9.185	1	25.33	H
ATOM	5255	HG12	ILE C	181	11.326	48.775	−9.285	1	21.74	H
ATOM	5256	HG13	ILE C	181	11.82	48.417	−10.749	1	21.74	H
ATOM	5257	HG21	ILE C	181	12.258	46.107	−11.395	1	23.73	H
ATOM	5258	HG22	ILE C	181	11.974	44.913	−10.386	1	23.73	H
ATOM	5259	HG23	ILE C	181	10.762	45.695	−11.053	1	23.73	H
ATOM	5260	HD11	ILE C	181	9.623	49.144	−10.808	1	30.93	H
ATOM	5261	HD12	ILE C	181	9.698	47.627	−11.274	1	30.93	H
ATOM	5262	HD13	ILE C	181	9.203	47.984	−9.807	1	30.93	H
ATOM	5263	N	ILE C	182	10.471	43.873	8.193	1	15.47	N
ATOM	5264	CA	ILE C	182	10.754	42.552	−7.654	1	15.31	C
ATOM	5265	C	ILE C	182	10.921	41.53	−8.77	1	20.29	C
ATOM	5266	O	ILE C	182	10.081	41.426	−9.662	1	15.6	O
ATOM	5267	CB	ILE C	182	9.631	42.095	−6.703	1	19.87	C
ATOM	5268	CG1	ILE C	182	9.419	43.135	−5.596	1	18.35	C
ATOM	5269	CG2	ILE C	182	9.959	40.735	6.096	1	17.54	C
ATOM	5270	CD1	ILE C	182	8.174	42.899	−4.758	1	19.47	C
ATOM	5271	H	ILE C	182	9.782	43.9	−8.707	1	18.56	H
ATOM	5272	HA	ILE C	182	11.582	42.586	−7.149	1	18.37	H
ATOM	5273	HB	ILE C	182	8.81	42.015	−7.212	1	23.85	H
ATOM	5274	HG12	ILE C	182	10.185	43.117	−5.001	1	22.02	H
ATOM	5275	HG13	ILE C	182	9.34	44.012	−6.003	1	22.02	H
ATOM	5276	HG21	ILE C	182	9.237	40.472	−5.504	1	21.04	H
ATOM	5277	HG22	ILE C	182	10.054	40.085	−6.811	1	21.04	H
ATOM	5278	HG23	ILE C	182	10.788	40.803	−5.598	1	21.04	H
ATOM	5279	HD11	ILE C	182	8.111	43.594	−4.084	1	23.36	H
ATOM	5280	HD12	ILE C	182	7.395	42.926	−5.335	1	23.36	H
ATOM	5281	HD13	ILE C	182	8.241	42.03	−4.331	1	23.36	H
ATOM	5282	N	GLU C	183	12.013	40.776	−8.717	1	17.61	N
ATOM	5283	CA	GLU C	183	12.211	39.676	−9.648	1	20.35	C
ATOM	5284	C	GLU C	183	11.144	38.62	−9.401	1	20.7	C
ATOM	5285	O	GLU C	183	10.829	38.289	−8.258	1	21.07	O
ATOM	5286	CB	GLU C	183	13.61	39.075	−9.5	1	26.3	C
ATOM	5287	CG	GLU C	183	14.73	40.031	−9.891	1	27.61	C
ATOM	5288	CD	GLU C	183	16.108	39.407	−9.763	1	38.86	C
ATOM	5289	OE1	GLU C	183	16.214	38.165	−9.858	1	36.41	O
ATOM	5290	OE2	GLU C	183	17.086	40.16	−9.564	1	42.7	O1−
ATOM	5291	H	GLU C	183	12.653	40.881	−8.152	1	21.14	H
ATOM	5292	HA	GLU C	183	12.114	40.002	−10.556	1	24.42	H
ATOM	5293	HB2	GLU C	183	13.746	38.821	−8.574	1	31.56	H
ATOM	5294	HB3	GLU C	183	13.676	38.292	−10.069	1	31.56	H
ATOM	5295	HG2	GLU C	183	14.607	40.3	−10.815	1	33.13	H
ATOM	5296	HG3	GLU C	183	14.697	40.809	−9.312	1	33.13	H
ATOM	5297	N	MET C	184	10.573	38.109	−10.482	1	22.39	N
ATOM	5298	CA	MET C	184	9.533	37.098	−10.391	1	21.6	C
ATOM	5299	C	MET C	184	9.735	36.135	−11.546	1	22.55	C
ATOM	5300	O	MET C	184	10.063	34.965	−11.347	1	23.79	O
ATOM	5301	CB	MET C	184	8.144	37.747	−10.426	1	20.97	C
ATOM	5302	CG	MET C	184	6.99	36.814	−10.069	1	19.42	C
ATOM	5303	SD	MET C	184	6.346	35.883	−11.472	1	22.46	S
ATOM	5304	CE	MET C	184	5.613	37.205	−12.438	1	23.45	C
ATOM	5305	H	MET C	184	10.773	38.334	−11.287	1	26.87	H
ATOM	5306	HA	MET C	184	9.624	36.618	−9.553	1	25.92	H
ATOM	5307	HB2	MET C	184	8.131	38.484	−9.796	1	25.17	H
ATOM	5308	HB3	MET C	184	7.983	38.082	−11.322	1	25.17	H
ATOM	5309	HG2	MET C	184	7.298	36.177	−9.405	1	23.3	H
ATOM	5310	HG3	MET C	184	6.263	37.343	−9.704	1	23.3	H
ATOM	5311	HE1	MET C	184	5.221	36.829	−13.241	1	28.15	H
ATOM	5312	HE2	MET C	184	4.927	37.64	−11.907	1	28.15	H
ATOM	5313	HE3	MET C	184	6.304	37.843	−12.674	1	28.15	H
ATOM	5314	N	GLN C	185	9.571	36.648	−12.758	1	18.88	N
ATOM	5315	CA	GLN C	185	9.795	35.862	−13.96	1	24.05	C
ATOM	5316	C	GLN C	185	10.736	36.628	−14.88	1	25.86	C
ATOM	5317	O	GLN C	185	10.834	37.853	−14.793	1	24.87	O
ATOM	5318	CB	GLN C	185	8.463	35.568	−14.648	1	25.95	C
ATOM	5319	CG	GLN C	185	8.465	34.367	−15.561	1	37.07	C
ATOM	5320	CD	GLN C	185	8.668	33.057	−14.826	1	34.64	C
ATOM	5321	OE1	GLN C	185	9.787	32.701	−14.462	1	43.56	O
ATOM	5322	NE2	GLN C	185	7.578	32.33	−14.609	1	35.6	N
ATOM	5323	H	GLN C	185	9.327	37.459	−12.911	1	22.66	H
ATOM	5324	HA	GLN C	185	10.213	35.019	−13.723	1	28.86	H
ATOM	5325	HB2	GLN C	185	7.791	35.416	−13.966	1	31.14	H
ATOM	5326	HB3	GLN C	185	8.215	36.34	−15.182	1	31.14	H
ATOM	5327	HG2	GLN C	185	7.612	34.322	−16.022	1	44.49	H
ATOM	5328	HG3	GLN C	185	9.184	34.463	−16.205	1	44.49	H
ATOM	5329	HE21	GLN C	185	7.639	31.578	−14.196	1	42.72	H
ATOM	5330	HE22	GLN C	185	6.812	32.611	−14.881	1	42.72	H
ATOM	5331	N	LYS C	186	11.446	35.921	−15.749	1	25.22	N
ATOM	5332	CA	LYS C	186	12.328	36.599	−16.689	1	33.47	C
ATOM	5333	C	LYS C	186	11.493	37.254	−17.785	1	26.33	C
ATOM	5334	O	LYS C	186	10.665	36.607	−18.428	1	24.54	O
ATOM	5335	CB	LYS C	186	13.351	35.63	−17.283	1	44.39	C
ATOM	5336	CG	LYS C	186	14.454	35.205	−16.308	1	62.35	C
ATOM	5337	CD	LYS C	186	15.252	36.385	−15.736	1	70.73	C
ATOM	5338	CE	LYS C	186	15.913	37.222	−16.825	1	85.5	C
ATOM	5339	NZ	LYS C	186	16.696	38.358	−16.263	1	92.86	N1+
ATOM	5340	H	LYS C	186	11.437	35.063	−15.816	1	30.26	H
ATOM	5341	HA	LYS C	186	12.812	37.298	−16.222	1	40.16	H
ATOM	5342	HB2	LYS C	186	12.889	34.829	−17.573	1	53.27	H
ATOM	5343	HB3	LYS C	186	13.778	36.056	−18.044	1	53.27	H
ATOM	5344	HG2	LYS C	186	14.05	34.732	−15.564	1	74.83	H
ATOM	5345	HG3	LYS C	186	15.075	34.622	−16.771	1	74.83	H
ATOM	5346	HD2	LYS C	186	14.653	36.961	−15.237	1	84.87	H
ATOM	5347	HD3	LYS C	186	15.949	36.044	−15.154	1	84.87	H
ATOM	5348	HE2	LYS C	186	16.519	36.66	−17.334	1	102.6	H
ATOM	5349	HE3	LYS C	186	15.228	37.586	−17.407	1	102.6	H
ATOM	5350	HZ1	LYS C	186	17.069	38.826	−16.922	1	111.43	H
ATOM	5351	HZ2	LYS C	186	16.161	38.893	−15.795	1	111.43	H
ATOM	5352	HZ3	LYS C	186	17.337	38.05	−15.729	1	111.43	H
ATOM	5353	N	GLY C	187	11.707	38.55	−17.977	1	22.7	N
ATOM	5354	CA	GLY C	187	10.938	39.312	−18.943	1	24.36	C
ATOM	5355	C	GLY C	187	11.284	40.784	−18.913	1	21.56	C
ATOM	5356	O	GLY C	187	12.096	41.226	−18.094	1	17.2	O
ATOM	5357	H	GLY C	187	12.298	39.013	−17.555	1	27.25	H
ATOM	5358	HA2	GLY C	187	11.111	38.972	−19.835	1	29.23	H
ATOM	5359	HA3	GLY C	187	9.991	39.213	−18.754	1	29.23	H
ATOM	5360	N	ASP C	188	10.659	41.544	−19.808	1	18.15	N
ATOM	5361	CA	ASP C	188	10.96	42.961	−19.96	1	17.36	C
ATOM	5362	C	ASP C	188	9.738	43.846	−19.697	1	19.06	C
ATOM	5363	O	ASP C	188	9.709	45.001	−20.117	1	15.87	O
ATOM	5364	CB	ASP C	188	11.509	43.226	−21.365	1	19.74	C
ATOM	5365	CG	ASP C	188	12.824	42.513	−21.618	1	23.22	C
ATOM	5366	OD1	ASP C	188	13.72	42.596	−20.754	1	19.57	O
ATOM	5367	OD2	ASP C	188	12.958	41.864	−22.675	1	26.62	O1−
ATOM	5368	H	ASP C	188	10.05	41.258	−20.344	1	21.78	H
ATOM	5369	HA	ASP C	188	11.648	43.206	−19.321	1	20.83	H
ATOM	5370	HB2	ASP C	188	10.866	42.914	−22.02	1	23.69	H
ATOM	5371	HB3	ASP C	188	11.657	44.179	−21.472	1	23.69	H
ATOM	5372	N	CYS C	189	8.739	43.299	−19.006	1	16.64	N
ATOM	5373	CA	CYS C	189	7.539	44.052	−18.63	1	17.86	C
ATOM	5374	C	CYS C	189	7.259	43.887	−17.138	1	16.95	C
ATOM	5375	O	CYS C	189	7.791	42.98	−16.504	1	15.25	O
ATOM	5376	CB	CYS C	189	6.326	43.596	−19.447	1	16.46	C
ATOM	5377	SG	CYS C	189	6.412	43.997	−21.213	1	19.92	S
ATOM	5378	H	CYS C	189	8.73	42.481	−18.739	1	19.97	H
ATOM	5379	HA	CYS C	189	7.686	44.995	−18.808	1	21.43	H
ATOM	5380	HB2	CYS C	189	6.245	42.632	−19.368	1	19.75	H
ATOM	5381	HB3	CYS C	189	5.532	44.021	−19.088	1	19.75	H
ATOM	5382	N	ALA C	190	6.424	44.763	−16.584	1	14.88	N
ATOM	5383	CA	ALA C	190	6.146	44.757	−15.149	1	15.16	C
ATOM	5384	C	ALA C	190	4.655	44.804	−14.854	1	12.33	C
ATOM	5385	O	ALA C	190	3.901	45.546	−15.487	1	12.28	O
ATOM	5386	CB	ALA C	190	6.845	45.927	−14.478	1	18.64	C
ATOM	5387	H	ALA C	190	6.003	45.373	−17.02	1	17.85	H
ATOM	5388	HA	ALA C	190	6.5	43.94	−14.766	1	18.19	H
ATOM	5389	HB1	ALA C	190	6.651	45.907	−13.528	1	22.37	H
ATOM	5390	HB2	ALA C	190	7.801	45.847	−14.622	1	22.37	H
ATOM	5391	HB3	ALA C	190	6.52	46.754	−14.866	1	22.37	H
ATOM	5392	N	LEU C	191	4.249	43.993	−13.882	1	10.76	N
ATOM	5393	CA	LEU C	191	2.888	43.985	−13.375	1	12.2	C
ATOM	5394	C	LEU C	191	2.805	44.849	−12.132	1	13.93	C
ATOM	5395	O	LEU C	191	3.653	44.741	−11.246	1	12.07	O
ATOM	5396	CB	LEU C	191	2.44	42.565	−13.034	1	11.91	C
ATOM	5397	CG	LEU C	191	2.3	41.584	−14.194	1	12.77	C
ATOM	5398	CD1	LEU C	191	2.254	40.162	−13.66	1	15.07	C
ATOM	5399	CD2	LEU C	191	1.046	41.904	−14.99	1	15.63	C
ATOM	5400	H	LEU C	191	4.761	43.423	−13.491	1	12.91	H
ATOM	5401	HA	LEU C	191	2.288	44.347	−14.046	1	14.65	H
ATOM	5402	HB2	LEU C	191	3.085	42.186	−12.416	1	14.29	H
ATOM	5403	HB3	LEU C	191	1.575	42.619	−12.599	1	14.29	H
ATOM	5404	HG	LEU C	191	3.066	41.667	−14.782	1	15.32	H
ATOM	5405	HD11	LEU C	191	2.165	39.548	−14.406	1	18.08	H
ATOM	5406	HD12	LEU C	191	3.076	39.98	−13.178	1	18.08	H
ATOM	5407	HD13	LEU C	191	1.494	40.073	−13.065	1	18.08	H
ATOM	5408	HD21	LEU C	191	0.969	41.274	−15.723	1	18.76	H
ATOM	5409	HD22	LEU C	191	0.275	41.829	−14.406	1	18.76	H
ATOM	5410	HD23	LEU C	191	1.114	42.808	−15.335	1	18.76	H
ATOM	5411	N	TYR C	192	1.786	45.698	−12.056	1	12.4	N
ATOM	5412	CA	TYR C	192	1.539	46.417	−10.818	1	15.75	C
ATOM	5413	C	TYR C	192	0.917	45.485	−9.793	1	13.37	C
ATOM	5414	O	TYR C	192	0.058	44.669	−10.119	1	12.8	O
ATOM	5415	CB	TYR C	192	0.619	47.621	−11.01	1	12.4	C
ATOM	5416	CG	TYR C	192	0.35	48.273	−9.679	1	17.77	C
ATOM	5417	CD1	TYR C	192	1.268	49.153	−9.128	1	19.33	C
ATOM	5418	CD2	TYR C	192	−0.786	47.958	−8.939	1	18.28	C
ATOM	5419	CE1	TYR C	192	1.051	49.729	−7.899	1	17.95	C
ATOM	5420	CE2	TYR C	192	−1.01	48.531	−7.701	1	20.59	C
ATOM	5421	CZ	TYR C	192	−0.085	49.416	−7.187	1	20.36	C
ATOM	5422	OH	TYR C	192	−0.287	49.996	−5.957	1	19.55	O
ATOM	5423	H	TYR C	192	1.236	45.873	−12.693	1	14.88	H
ATOM	5424	HA	TYR C	192	2.383	46.736	−10.463	1	18.89	H
ATOM	5425	HB2	TYR C	192	1.047	48.268	−11.591	1	14.88	H
ATOM	5426	HB3	TYR C	192	−0.226	47.329	−11.388	1	14.88	H
ATOM	5427	HD1	TYR C	192	2.038	49.366	−9.603	1	23.2	H
ATOM	5428	HD2	TYR C	192	−1.407	47.36	−9.286	1	21.93	H
ATOM	5429	HE1	TYR C	192	1.673	50.325	−7.548	1	21.53	H
ATOM	5430	HE2	TYR C	192	−1.777	48.322	−7.219	1	24.7	H
ATOM	5431	HH	TYR C	192	−1.011	49.725	−5.627	1	23.47	H
ATOM	5432	N	ALA C	193	1.363	45.625	−8.552	1	14.31	N
ATOM	5433	CA	ALA C	193	0.773	44.931	−7.416	1	14.94	C
ATOM	5434	C	ALA C	193	0.867	45.856	6.211	1	17.89	C
ATOM	5435	O	ALA C	193	1.874	46.539	−6.034	1	18.07	O
ATOM	5436	CB	ALA C	193	1.488	43.614	−7.146	1	13.51	C
ATOM	5437	H	ALA C	193	2.025	46.13	−8.337	1	17.18	H
ATOM	5438	HA	ALA C	193	0.162	44.747	−7.595	1	17.93	H
ATOM	5439	HB1	ALA C	193	1.071	43.179	−6.386	1	16.22	H
ATOM	5440	HB2	ALA C	193	1.416	43.05	−7.932	1	16.22	H
ATOM	5441	HB3	ALA C	193	2.421	43.796	−6.954	1	16.22	H
ATOM	5442	N	SER C	194	−0.171	45.893	−5.385	1	15.21	N
ATOM	5443	CA	SER C	194	−0.15	46.773	−4.22	1	19.46	C
ATOM	5444	C	SER C	194	0.589	46.101	−3.063	1	18.48	C
ATOM	5445	O	SER C	194	0.561	44.878	−2.952	1	20	O
ATOM	5446	CB	SER C	194	−1.569	47.149	−3.798	1	18.63	C
ATOM	5447	OG	SER C	194	−2.308	45.998	−3.45	1	27.89	O
ATOM	5448	H	SER C	194	−0.889	45.428	−5.472	1	18.26	H
ATOM	5449	HA	SER C	194	0.323	47.589	−4.447	1	23.36	H
ATOM	5450	HB2	SER C	194	−1.525	47.74	−3.03	1	22.35	H
ATOM	5451	HB3	SER C	194	−2.011	47.596	−4.537	1	22.35	H
ATOM	5452	HG	SER C	194	−1.935	45.6	−2.811	1	33.47	H
ATOM	5453	N	SER C	195	1.243	46.877	−2.197	1	20.9	N
ATOM	5454	CA	SER C	195	1.276	48.334	−2.265	1	24.71	C
ATOM	5455	C	SER C	195	2.483	48.832	−3.053	1	20.24	C
ATOM	5456	O	SER C	195	3.625	48.682	−2.618	1	19.16	O
ATOM	5457	CB	SER C	195	1.3	48.929	−0.858	1	22.44	C
ATOM	5458	OG	SER C	195	1.256	50.341	−0.92	1	28.76	O
ATOM	5459	H	SER C	195	1.694	46.564	−1.535	1	25.08	H
ATOM	5460	HA	SER C	195	0.474	48.648	−2.712	1	29.65	H
ATOM	5461	HB2	SER C	195	0.528	48.609	−0.365	1	26.93	H
ATOM	5462	HB3	SER C	195	2.117	48.656	−0.412	1	26.93	H
ATOM	5463	HG	SER C	195	1.27	50.663	−0.144	1	34.51	H
ATOM	5464	N	PHE C	196	2.215	49.423	4.213	1	20.32	N
ATOM	5465	CA	PHE C	196	3.249	50.046	−5.035	1	19.27	C
ATOM	5466	C	PHE C	196	4.443	49.138	−5.29	1	23.51	C
ATOM	5467	O	PHE C	196	5.581	49.456	−4.933	1	18.74	O
ATOM	5468	CB	PHE C	196	3.708	51.345	−4.384	1	20.31	C
ATOM	5469	CG	PHE C	196	2.685	52.432	−4.451	1	21.15	C
ATOM	5470	CD1	PHE C	196	2.543	53.189	−5.599	1	21.62	C
ATOM	5471	CD2	PHE C	196	1.849	52.685	3.378	1	27.55	C
ATOM	5472	CE1	PHE C	196	1.592	54.182	−5.673	1	19.96	C
ATOM	5473	CE2	PHE C	196	0.899	53.68	−3.447	1	23.4	C
ATOM	5474	CZ	PHE C	196	0.772	54.43	−4.595	1	21.78	C
ATOM	5475	H	PHE C	196	1.427	49.477	−4.553	1	24.38	H
ATOM	5476	HA	PHE C	196	2.864	50.271	−5.896	1	23.12	H
ATOM	5477	HB2	PHE C	196	3.902	51.176	−3.448	1	24.38	H
ATOM	5478	HB3	PHE C	196	4.507	51.658	−4.836	1	24.38	H
ATOM	5479	HD1	PHE C	196	3.095	53.025	−6.329	1	25.94	H
ATOM	5480	HD2	PHE C	196	1.932	52.181	−2.601	1	33.05	H
ATOM	5481	HE1	PHE C	196	1.508	54.688	−6.448	1	23.95	H
ATOM	5482	HE2	PHE C	196	0.345	53.846	−2.719	1	28.08	H
ATOM	5483	HZ	PHE C	196	0.131	55.102	4.643	1	26.14	H
ATOM	5484	N	LYS C	197	4.165	48.003	−5.919	1	18	N
ATOM	5485	CA	LYS C	197	5.197	47.054	6.288	1	21.33	C
ATOM	5486	C	LYS C	197	5.092	46.769	7.776	1	18.93	C
ATOM	5487	0	LYS C	197	4.018	46.905	−8.367	1	15.6	O
ATOM	5488	CB	LYS C	197	5.064	45.765	−5.474	1	21.85	C
ATOM	5489	CG	LYS C	197	4.958	46.002	−3.977	1	27.27	C
ATOM	5490	CD	LYS C	197	5.109	44.719	−3.183	1	29.38	C
ATOM	5491	CE	LYS C	197	3.988	43.739	−3.459	1	32.12	C
ATOM	5492	NZ	LYS C	197	4.083	42.54	−2.575	1	44.07	N1+
ATOM	5493	H	LYS C	197	3.372	47.759	−6.146	1	21.6	H
ATOM	5494	HA	LYS C	197	6.069	47.44	−6.11	1	25.6	H
ATOM	5495	HB2	LYS C	197	4.264	45.296	−5.759	1	26.23	H
ATOM	5496	HB3	LYS C	197	5.844	45.212	−5.634	1	26.23	H
ATOM	5497	HG2	LYS C	197	5.66	46.612	−3.702	1	32.72	H
ATOM	5498	HG3	LYS C	197	4.089	46.381	−3.776	1	32.72	H
ATOM	5499	HD2	LYS C	197	5.948	44.294	−3.422	1	35.26	H
ATOM	5500	HD3	LYS C	197	5.1	44.929	2.236	1	35.26	H
ATOM	5501	HE2	LYS C	197	3.135	44.172	3.295	1	38.55	H
ATOM	5502	HE3	LYS C	197	4.042	43.442	−4.381	1	38.55	H
ATOM	5503	HZ1	LYS C	197	3.416	41.977	−2.752	1	52.89	H
ATOM	5504	HZ2	LYS C	197	4.857	42.123	−2.71	1	52.89	H
ATOM	5505	HZ3	LYS C	197	4.033	42.787	−1.721	1	52.89	H
ATOM	5506	N	GLY C	198	6.222	46.404	−8.372	1	13.97	N
ATOM	5507	CA	GLY C	198	6.273	45.977	−9.754	1	12.15	C
ATOM	5508	C	GLY C	198	6.935	44.618	−9.848	1	15.82	C
ATOM	5509	O	GLY C	198	8.119	44.484	−9.54	1	16.91	O
ATOM	5510	H	GLY C	198	6.988	46.398	−7.982	1	16.76	H
ATOM	5511	HA2	GLY C	198	5.375	45.916	−10.116	1	14.58	H
ATOM	5512	HA3	GLY C	198	6.783	46.613	−10.28	1	14.58	H
ATOM	5513	N	TYR C	199	6.172	43.605	−10.251	1	14.27	N
ATOM	5514	CA	TYR C	199	6.716	42.267	−10.466	1	14.6	C
ATOM	5515	C	TYR C	199	7.146	42.099	−11.92	1	15.48	C
ATOM	5516	O	TYR C	199	6.36	42.327	−12.829	1	12.77	O
ATOM	5517	CB	TYR C	199	5.689	41.192	−10.101	1	14.93	C
ATOM	5518	CG	TYR C	199	5.489	41.006	−8.615	1	20.52	C
ATOM	5519	CD1	TYR C	199	6.359	40.22	−7.87	1	15.96	C
ATOM	5520	CD2	TYR C	199	4.425	41.609	−7.956	1	18.27	C
ATOM	5521	CE1	TYR C	199	6.179	40.044	−6.509	1	18.35	C
ATOM	5522	CE2	TYR C	199	4.236	41.438	−6.596	1	20.42	C
ATOM	5523	CZ	TYR C	199	5.116	40.654	−5.877	1	22.28	C
ATOM	5524	OH	TYR C	199	4.931	40.486	−4.522	1	27.53	O
ATOM	5525	H	TYR C	199	5.329	43.667	−10.408	1	17.12	H
ATOM	5526	HA	TYR C	199	7.496	42.145	−9.903	1	17.52	H
ATOM	5527	HB2	TYR C	199	4.833	41.436	−10.486	1	17.92	H
ATOM	5528	HB3	TYR C	199	5.983	40.344	−10.468	1	17.92	H
ATOM	5529	HD1	TYR C	199	7.077	39.807	−8.293	1	19.15	H
ATOM	5530	HD2	TYR C	199	3.83	42.137	−8.438	1	21.93	H
ATOM	5531	HE1	TYR C	199	6.771	39.517	−6.024	1	22.01	H
ATOM	5532	HE2	TYR C	199	3.52	41.849	−6.168	1	24.5	H
ATOM	5533	HH	TYR C	199	4.251	40.909	−4.27	1	33.04	H
ATOM	5534	N	ILE C	200	8.396	41.698	−12.128	1	16.81	N
ATOM	5535	CA	ILE C	200	8.926	41.482	−13.471	1	15.74	C
ATOM	5536	C	ILE C	200	8.28	40.245	−14.1	1	16.52	C
ATOM	5537	O	ILE C	200	8.284	39.168	−13.505	1	15.2	O
ATOM	5538	CB	ILE C	200	10.46	41.318	−13.442	1	16.14	C
ATOM	5539	CG1	ILE C	200	11.1	42.522	−12.738	1	15.26	C
ATOM	5540	CG2	ILE C	200	11.01	41.152	−14.861	1	16.45	C
ATOM	5541	CD1	ILE C	200	12.613	42.437	−12.586	1	18.39	C
ATOM	5542	H	ILE C	200	8.964	41.543	−11.501	1	20.17	H
ATOM	5543	HA	ILE C	200	8.713	42.249	−14.025	1	18.88	H
ATOM	5544	HB	ILE C	200	10.673	40.519	−12.936	1	19.37	H
ATOM	5545	HG12	ILE C	200	10.9	43.322	−13.249	1	18.31	H
ATOM	5546	HG13	ILE C	200	10.719	42.6	−11.849	1	18.31	H
ATOM	5547	HG21	ILE C	200	11.974	41.051	−14.816	1	19.74	H
ATOM	5548	HG22	ILE C	200	10.613	40.363	−15.263	1	19.74	H
ATOM	5549	HG23	ILE C	200	10.784	41.939	−15.381	1	19.74	H
ATOM	5550	HD11	ILE C	200	12.93	43.234	−12.133	1	22.06	H
ATOM	5551	HD12	ILE C	200	12.834	41.65	−12.064	1	22.06	H
ATOM	5552	HD13	ILE C	200	13.016	42.374	−13.466	1	22.06	H
ATOM	5553	N	GLU C	201	7.728	40.405	−15.302	1	15.15	N
ATOM	5554	CA	GLU C	201	6.998	39.327	−15.966	1	17.24	C
ATOM	5555	C	GLU C	201	7.281	39.288	−17.467	1	21.31	C
ATOM	5556	O	GLU C	201	7.635	40.302	−18.076	1	15.67	O
ATOM	5557	CB	GLU C	201	5.491	39.485	−15.712	1	17.25	C
ATOM	5558	CG	GLU C	201	4.6	38.46	−16.405	1	20.61	C
ATOM	5559	CD	GLU C	201	4.918	37.025	−16.012	1	24.32	C
ATOM	5560	OE1	GLU C	201	5.957	36.492	−16.457	1	24.36	O
ATOM	5561	OE2	GLU C	201	4.12	36.426	−15.262	1	26.94	O1−
ATOM	5562	H	GLU C	201	7.763	41.134	−15.757	1	18.18	H
ATOM	5563	HA	GLU C	201	7.277	38.479	−15.587	1	20.69	H
ATOM	5564	HB2	GLU C	201	5.33	39.412	−14.758	1	20.7	H
ATOM	5565	HB3	GLU C	201	5.218	40.364	−16.02	1	20.7	H
ATOM	5566	HG2	GLU C	201	3.676	38.637	−16.17	1	24.73	H
ATOM	5567	HG3	GLU C	201	4.718	38.54	−17.365	1	24.73	H
ATOM	5568	N	ASN C	202	7.143	38.099	−18.05	1	18.71	N
ATOM	5569	CA	ASN C	202	7.219	37.925	−19.497	1	20.17	C
ATOM	5570	C	ASN C	202	6.078	38.663	−20.179	1	18.49	C
ATOM	5571	O	ASN C	202	4.912	38.461	−19.844	1	16.77	O
ATOM	5572	CB	ASN C	202	7.176	36.435	−19.857	1	23.56	C
ATOM	5573	CG	ASN C	202	7.406	36.177	−21.341	1	23.4	C
ATOM	5574	OD1	ASN C	202	6.838	36.85	−22.202	1	21.3	O
ATOM	5575	ND2	ASN C	202	8.248	35.191	−21.643	1	23.28	N
ATOM	5576	H	ASN C	202	7.002	37.368	−17.621	1	22.45	H
ATOM	5577	HA	ASN C	202	8.056	38.292	−19.821	1	24.21	H
ATOM	5578	HB2	ASN C	202	7.869	35.971	−19.362	1	28.27	H
ATOM	5579	HB3	ASN C	202	6.305	36.079	−19.623	1	28.27	H
ATOM	5580	HD21	ASN C	202	8.413	35.004	−22.466	1	27.94	H
ATOM	5581	HD22	ASN C	202	8.626	34.741	−21.015	1	27.94	H
ATOM	5582	N	CYS C	203	6.418	39.501	−21.153	1	15.62	N
ATOM	5583	CA	CYS C	203	5.443	40.379	−21.787	1	17.19	C
ATOM	5584	C	CYS C	203	4.362	39.611	−22.551	1	21.25	C
ATOM	5585	O	CYS C	203	3.338	40.187	−22.922	1	19.77	O
ATOM	5586	CB	CYS C	203	6.159	41.353	−22.727	1	20.68	C
ATOM	5587	SG	CYS C	203	7.423	42.375	−21.911	1	23.41	S
ATOM	5588	H	CYS C	203	7.215	39.58	−21.467	1	18.74	H
ATOM	5589	HA	CYS C	203	5.003	40.902	−21.099	1	20.63	H
ATOM	5590	HB2	CYS C	203	6.596	40.846	−23.428	1	24.82	H
ATOM	5591	HB3	CYS C	203	5.501	41.951	−23.115	1	24.82	H
ATOM	5592	N	SER C	204	4.585	38.317	−22.774	1	16.75	N
ATOM	5593	CA	SER C	204	3.614	37.469	−23.47	1	19.18	C
ATOM	5594	C	SER C	204	2.544	36.908	−22.539	1	19.81	C
ATOM	5595	O	SER C	204	1.558	36.328	−22.991	1	19.37	O
ATOM	5596	CB	SER C	204	4.327	36.306	−24.161	1	22.12	C
ATOM	5597	OG	SER C	204	5.221	36.785	−25.144	1	22.09	O
ATOM	5598	H	SER C	204	5.297	37.901	−22.53	1	20.11	H
ATOM	5599	HA	SER C	204	3.169	37.996	−24.152	1	23.02	H
ATOM	5600	HB2	SER C	204	4.825	35.802	−23.499	1	26.54	H
ATOM	5601	HB3	SER C	204	3.666	35.737	−24.585	1	26.54	H
ATOM	5602	HG	SER C	204	5.799	37.281	−24.789	1	26.51	H
ATOM	5603	N	THR C	205	2.747	37.067	−21.237	1	15.82	N
ATOM	5604	CA	THR C	205	1.848	36.478	−20.254	1	17.27	C
ATOM	5605	C	THR C	205	0.512	37.224	−20.2	1	23.16	C
ATOM	5606	O	THR C	205	0.486	38.427	−19.927	1	18.56	O
ATOM	5607	CB	THR C	205	2.486	36.48	−18.855	1	20.49	C
ATOM	5608	OG1	THR C	205	3.798	35.907	−18.927	1	19.75	O
ATOM	5609	CG2	THR C	205	1.643	35.677	−17.877	1	22.93	C
ATOM	5610	H	THR C	205	3.399	37.513	−20.897	1	18.99	H
ATOM	5611	HA	THR C	205	1.669	35.557	−20.501	1	20.72	H
ATOM	5612	HB	THR C	205	2.549	37.392	−18.53	1	24.58	H
ATOM	5613	HG1	THR C	205	3.751	35.117	−19.208	1	23.7	H
ATOM	5614	HG21	THR C	205	2.055	35.686	−16.999	1	27.51	H
ATOM	5615	HG22	THR C	205	0.754	36.061	−17.812	1	27.51	H
ATOM	5616	HG23	THR C	205	1.568	34.759	−18.181	1	27.51	H
ATOM	5617	N	PRO C	206	−0.604	36.517	−20.459	1	17.76	N
ATOM	5618	CA	PRO C	206	−1.898	37.193	−20.323	1	19.8	C
ATOM	5619	C	PRO C	206	−2.147	37.676	−18.898	1	20.72	C
ATOM	5620	O	PRO C	206	−1.969	36.923	−17.94	1	18.27	O
ATOM	5621	CB	PRO C	206	−2.913	36.112	−20.718	1	22.87	C
ATOM	5622	CG	PRO C	206	−2.139	35.122	−21.513	1	28.25	C
ATOM	5623	CD	PRO C	206	−0.76	35.128	−20.926	1	20.21	C
ATOM	5624	HA	PRO C	206	−1.96	37.941	−20.939	1	23.76	H
ATOM	5625	HB2	PRO C	206	−3.278	35.7	−19.919	1	27.44	H
ATOM	5626	HB3	PRO C	206	−3.618	36.506	−21.255	1	27.44	H
ATOM	5627	HG2	PRO C	206	−2.544	34.245	−21.425	1	33.91	H
ATOM	5628	HG3	PRO C	206	−2.116	35.397	−22.443	1	33.91	H
ATOM	5629	HD2	PRO C	206	−0.707	34.511	−20.18	1	24.25	H
ATOM	5630	HD3	PRO C	206	−0.101	34.923	−21.608	1	24.25	H
ATOM	5631	N	ASN C	207	−2.542	38.936	−18.774	1	19.76	N
ATOM	5632	CA	ASN C	207	−2.912	39.512	−17.49	1	19.32	C
ATOM	5633	C	ASN C	207	−3.985	40.567	−17.689	1	19.48	C
ATOM	5634	O	ASN C	207	−4.119	41.121	−18.782	1	15.57	O
ATOM	5635	CB	ASN C	207	−1.701	40.14	−16.796	1	18.33	C
ATOM	5636	CG	ASN C	207	−0.82	39.12	−16.109	1	16.71	C
ATOM	5637	OD1	ASN C	207	−1.106	38.69	−14.991	1	18.99	O
ATOM	5638	ND2	ASN C	207	0.266	38.735	−16.768	1	18.7	N
ATOM	5639	H	ASN C	207	−2.604	39.487	−19.431	1	23.72	H
ATOM	5640	HA	ASN C	207	−3.268	38.816	−16.915	1	23.19	H
ATOM	5641	HB2	ASN C	207	−1.163	40.603	−17.457	1	21.99	H
ATOM	5642	HB3	ASN C	207	−2.013	40.767	−16.124	1	21.99	H
ATOM	5643	HD21	ASN C	207	0.799	38.157	−16.42	1	22.44	H
ATOM	5644	HD22	ASN C	207	0.437	39.064	−17.544	1	22.44	H
ATOM	5645	N	THR C	208	−4.742	40.847	−16.634	1	16.68	N
ATOM	5646	CA	THR C	208	−5.613	42.012	−16.63	1	15.95	C
ATOM	5647	C	THR C	208	−4.721	43.246	−16.681	1	17.24	C
ATOM	5648	O	THR C	208	−3.514	43.148	−16.471	1	15.69	O
ATOM	5649	CB	THR C	208	−6.522	42.041	−15.393	1	19.27	C
ATOM	5650	OG1	THR C	208	−5.725	42.005	−14.204	1	15.59	O
ATOM	5651	CG2	THR C	208	−7.471	40.844	−15.408	1	21.85	C
ATOM	5652	H	THR C	208	−4.77	40.38	−15.912	1	20.02	H
ATOM	5653	HA	THR C	208	−6.172	42.003	−17.423	1	19.14	H
ATOM	5654	HB	THR C	208	−7.053	42.853	−15.402	1	23.12	H
ATOM	5655	HG1	THR C	208	−6.22	42.021	−13.525	1	18.71	H
ATOM	5656	HG21	THR C	208	−8.044	40.866	−14.625	1	26.22	H
ATOM	5657	HG22	THR C	208	−8.025	40.869	−16.204	1	26.22	H
ATOM	5658	HG23	THR C	208	−6.963	40.018	−15.403	1	26.22	H
ATOM	5659	N	TYR C	209	−5.292	44.405	−16.979	1	16.72	N
ATOM	5660	CA	TYR C	209	−4.47	45.597	−17.141	1	13.53	C
ATOM	5661	C	TYR C	209	−5.203	46.876	−16.759	1	14.4	C
ATOM	5662	O	TYR C	209	−6.437	46.914	−16.687	1	12.53	O
ATOM	5663	CB	TYR C	209	−3.958	45.689	−18.585	1	14.96	C
ATOM	5664	CG	TYR C	209	−5.04	45.726	−19.649	1	18.5	C
ATOM	5665	CD1	TYR C	209	−5.741	44.58	−19.996	1	19.53	C
ATOM	5666	CD2	TYR C	209	−5.343	46.907	−20.318	1	14.68	C
ATOM	5667	CE1	TYR C	209	−6.723	44.609	−20.97	1	19.93	C
ATOM	5668	CE2	TYR C	209	−6.317	46.947	−21.291	1	21.82	C
ATOM	5669	CZ	TYR C	209	−7.005	45.797	−21.615	1	26.03	C
ATOM	5670	OH	TYR C	209	−7.976	45.843	−22.585	1	20.92	O
ATOM	5671	H	TYR C	209	−6.136	44.528	−17.09	1	20.07	H
ATOM	5672	HA	TYR C	209	−3.696	45.52	−16.561	1	16.23	H
ATOM	5673	HB2	TYR C	209	−3.432	46.5	−18.675	1	17.95	H
ATOM	5674	HB3	TYR C	209	−3.399	44.917	−18.764	1	17.95	H
ATOM	5675	HD1	TYR C	209	−5.551	43.78	−19.562	1	23.43	H
ATOM	5676	HD2	TYR C	209	−4.881	47.685	−20.102	1	17.62	H
ATOM	5677	HE1	TYR C	209	−7.187	43.834	−21.191	1	23.92	H
ATOM	5678	HE2	TYR C	209	−6.511	47.745	−21.727	1	26.18	H
ATOM	5679	HH	TYR C	209	−8.317	45.082	−22.686	1	25.1	H
ATOM	5680	N	ILE C	210	−4.411	47.914	−16.502	1	12.1	N
ATOM	5681	CA	ILE C	210	−4.92	49.213	−16.091	1	14.56	C
ATOM	5682	C	ILE C	210	−4.546	50.283	−17.113	1	16.31	C
ATOM	5683	O	ILE C	210	−3.369	50.482	−17.419	1	14.03	O
ATOM	5684	CB	ILE C	210	−4.37	49.618	−14.707	1	15.33	C
ATOM	5685	CG1	ILE C	210	−4.746	48.564	−13.661	1	15.55	C
ATOM	5686	CG2	ILE C	210	−4.904	50.989	−14.3	1	16.97	C
ATOM	5687	CD1	ILE C	210	−4.066	48.749	−12.314	1	17.1	C
ATOM	5688	H	ILE C	210	−3.554	47.886	−16.562	1	14.52	H
ATOM	5689	HA	ILE C	210	−5.887	49.174	−16.033	1	17.47	H
ATOM	5690	HB	ILE C	210	−3.403	49.667	−14.761	1	18.39	H
ATOM	5691	HG12	ILE C	210	−5.704	48.599	−13.515	1	18.66	H
ATOM	5692	HG13	ILE C	210	−4.498	47.689	−13.998	1	18.66	H
ATOM	5693	HG21	ILE C	210	−4.546	51.222	−13.429	1	20.36	H
ATOM	5694	HG22	ILE C	210	−4.625	51.645	−14.958	1	20.36	H
ATOM	5695	HG23	ILE C	210	−5.873	50.951	−14.26	1	20.36	H
ATOM	5696	HD11	ILE C	210	−4.357	48.045	−11.714	1	20.51	H
ATOM	5697	HD12	ILE C	210	−3.105	48.704	−12.437	1	20.51	H
ATOM	5698	HD13	ILE C	210	−4.313	49.615	−11.953	1	20.51	H
ATOM	5699	N	CYS C	211	−5.558	50.963	−17.639	1	16.07	N
ATOM	5700	CA	CYS C	211	−5.348	52.082	−18.544	1	16.5	C
ATOM	5701	C	CYS C	211	−5.448	53.379	−17.768	1	16.84	C
ATOM	5702	0	CYS C	211	−6.188	53.471	−16.787	1	17.47	O
ATOM	5703	CB	CYS C	211	6.366	52.068	−19.685	1	24.73	C
ATOM	5704	SG	CYS C	211	−6.116	50.73	−20.874	1	30.48	S
ATOM	5705	H	CYS C	211	6.386	50.791	−17.484	1	19.28	H
ATOM	5706	HA	CYS C	211	−4.459	52.023	−18.927	1	19.81	H
ATOM	5707	HB2	CYS C	211	−7.255	51.969	−19.31	1	29.68	H
ATOM	5708	HB3	CYS C	211	−6.305	52.908	−20.167	1	29.68	H
ATOM	5709	N	MET C	212	−4.706	54.38	−18.222	1	19.38	N
ATOM	5710	CA	MET C	212	−4.653	55.668	−17.551	1	17.22	C
ATOM	5711	C	MET C	212	−4.669	56.802	−18.563	1	21.46	C
ATOM	5712	O	MET C	212	−4.066	56.699	−19.634	1	19.72	O
ATOM	5713	CB	MET C	212	−3.402	55.756	−16.681	1	17.06	C
ATOM	5714	CG	MET C	212	−3.232	57.075	−15.955	1	20.46	C
ATOM	5715	SD	MET C	212	−1.732	57.072	−14.95	1	22.92	S
ATOM	5716	CE	MET C	212	−1.636	58.792	−14.465	1	27.66	C
ATOM	5717	H	MET C	212	−4.217	54.337	−18.928	1	23.26	H
ATOM	5718	HA	MET C	212	−5.426	55.752	−16.971	1	20.66	H
ATOM	5719	HB2	MET C	212	−3.439	55.054	−16.013	1	20.47	H
ATOM	5720	HB3	MET C	212	−2.623	55.628	−17.245	1	20.47	H
ATOM	5721	HG2	MET C	212	−3.164	57.793	−16.603	1	24.55	H
ATOM	5722	HG3	MET C	212	−3.992	57.22	−15.369	1	24.55	H
ATOM	5723	HE1	MET C	212	−1.569	59.341	−15.262	1	33.19	H
ATOM	5724	HE2	MET C	212	−2.436	59.025	−13.968	1	33.19	H
ATOM	5725	HE3	MET C	212	−0.852	58.919	−13.908	1	33.19	H
ATOM	5726	N	GLN C	213	−5.37	57.878	−18.219	1	17.77	N
ATOM	5727	CA	GLN C	213	−5.404	59.079	−19.048	1	25.12	C
ATOM	5728	C	GLN C	213	−5.4	60.318	−18.16	1	26.47	C
ATOM	5729	O	GLN C	213	−6.282	60.489	−17.319	1	26.02	O
ATOM	5730	CB	GLN C	213	−6.639	59.08	−19.953	1	26.62	C
ATOM	5731	CG	GLN C	213	−6.655	60.187	−20.999	1	29.95	C
ATOM	5732	CD	GLN C	213	−8.002	60.315	−21.689	1	32.31	C
ATOM	5733	OE1	GLN C	213	−8.926	60.93	−21.157	1	30.11	O
ATOM	5734	NE2	GLN C	213	−8.121	59.727	−22.874	1	31.23	N
ATOM	5735	H	GLN C	213	−5.84	57.938	−17.502	1	21.33	H
ATOM	5736	HA	GLN C	213	−4.614	59.103	−19.61	1	30.14	H
ATOM	5737	HB2	GLN C	213	−6.682	58.232	−20.421	1	31.94	H
ATOM	5738	HB3	GLN C	213	−7.429	59.188	−19.4	1	31.94	H
ATOM	5739	HG2	GLN C	213	−6.456	61.033	−20.568	1	35.94	H
ATOM	5740	HG3	GLN C	213	−5.987	59.993	−21.676	1	35.94	H
ATOM	5741	HE21	GLN C	213	−7.455	59.302	−23.213	1	37.48	H
ATOM	5742	HE22	GLN C	213	−8.865	59.772	−23.304	1	37.48	H
ATOM	5743	N	ARG C	214	−4.398	61.171	−18.344	1	27.5	N
ATOM	5744	CA	ARG C	214	−4.329	62.438	−17.626	1	31.88	C
ATOM	5745	C	ARG C	214	−5.318	63.436	−18.229	1	33.93	C
ATOM	5746	O	ARG C	214	−5.446	63.533	−19.451	1	35.59	O
ATOM	5747	CB	ARG C	214	−2.905	62.994	−17.664	1	40.82	C
ATOM	5748	CG	ARG C	214	−1.878	62.073	−17.022	1	40.28	C
ATOM	5749	CD	ARG C	214	−0.473	62.643	−17.093	1	53.54	C
ATOM	5750	NE	ARG C	214	−0.373	63.945	−16.438	1	62.54	N
ATOM	5751	CZ	ARG C	214	−0.186	64.121	−15.133	1	62.56	C
ATOM	5752	NH1	ARG C	214	−0.083	63.078	−14.32	1	49.8	N1+
ATOM	5753	NH2	ARG C	214	−0.106	65.349	−14.635	1	61.54	N
ATOM	5754	H	ARG C	214	−3.741	61.038	−18.883	1	33	H
ATOM	5755	HA	ARG C	214	−4.573	62.293	−16.699	1	38.26	H
ATOM	5756	HB2	ARG C	214	−2.647	63.131	−18.588	1	48.98	H
ATOM	5757	HB3	ARG C	214	−2.886	63.839	−17.187	1	48.98	H
ATOM	5758	HG2	ARG C	214	−2.104	61.945	−16.088	1	48.33	H
ATOM	5759	HG3	ARG C	214	−1.881	61.221	−17.487	1	48.33	H
ATOM	5760	HD2	ARG C	214	0.14	62.035	−16.651	1	64.25	H
ATOM	5761	HD3	ARG C	214	−0.221	62.753	−18.024	1	64.25	H
ATOM	5762	HE	ARG C	214	−0.44	64.647	−16.931	1	75.04	H
ATOM	5763	HH11	ARG C	214	−0.133	62.279	−14.636	1	59.76	H
ATOM	5764	HH12	ARG C	214	0.037	63.199	−13.477	1	59.76	H
ATOM	5765	HH21	ARG C	214	−0.174	66.03	−15.157	1	73.85	H
ATOM	5766	HH22	ARG C	214	0.012	65.465	−13.791	1	73.85	H
ATOM	5767	N	THR C	215	−6.025	64.167	−17.372	1	36.74	N
ATOM	5768	CA	THR C	215	−7.027	65.127	−17.832	1	41.57	C
ATOM	5769	C	THR C	215	−6.376	66.389	−18.393	1	37.21	C
ATOM	5770	O	THR C	215	−5.421	66.913	−17.819	1	43.79	O
ATOM	5771	CB	THR C	215	−7.992	65.528	−16.697	1	37.58	C
ATOM	5772	OG1	THR C	215	−7.256	66.123	−15.621	1	31.78	O
ATOM	5773	CG2	THR C	215	−8.75	64.313	−16.184	1	39.25	C
ATOM	5774	H	THR C	215	−5.945	64.125	−16.517	1	44.09	H
ATOM	5775	HA	THR C	215	−7.551	64.721	−18.54	1	49.88	H
ATOM	5776	HB	THR C	215	−8.637	66.169	−17.036	1	45.09	H
ATOM	5777	HG1	THR C	215	−6.693	65.577	−15.322	1	38.13	H
ATOM	5778	HG21	THR C	215	−9.354	64.576	−15.471	1	47.1	H
ATOM	5779	HG22	THR C	215	−9.266	63.916	−16.903	1	47.1	H
ATOM	5780	HG23	THR C	215	−8.126	63.654	−15.841	1	47.1	H
TER	5781		THR C	215
ATOM	5782	N	GLU D	93	−16.518	60.935	−24.144	1	50.72	N
ATOM	5783	CA	GLU D	93	−15.948	61.865	−23.176	1	55.05	C
ATOM	5784	C	GLU D	93	−17.021	62.338	−22.2	1	56.26	C
ATOM	5785	O	GLU D	93	−18.143	62.642	−22.604	1	53.3	O
ATOM	5786	CB	GLU D	93	−15.318	63.062	−23.888	1	63.84	C
ATOM	5787	CG	GLU D	93	−14.372	63.872	−23.016	1	63.9	C
ATOM	5788	CD	GLU D	93	−13.844	65.113	−23.716	1	77.81	C
ATOM	5789	OE1	GLU D	93	−14.545	65.642	−24.605	1	77.09	O
ATOM	5790	OE2	GLU D	93	−12.725	65.558	−23.379	1	78.31	O1−
ATOM	5791	HA	GLU D	93	−15.255	61.413	−22.669	1	66.06	H
ATOM	5792	HB2	GLU D	93	−14.813	62.74	−24.651	1	76.6	H
ATOM	5793	HB3	GLU D	93	−16.025	63.654	−24.188	1	76.6	H
ATOM	5794	HG2	GLU D	93	−14.844	64.157	−22.217	1	76.68	H
ATOM	5795	HG3	GLU D	93	−13.613	63.319	−22.773	1	76.68	H
ATOM	5796	N	SER D	94	−16.675	62.405	−20.918	1	45.44	N
ATOM	5797	CA	SER D	94	−17.646	62.768	−19.894	1	42.83	C
ATOM	5798	C	SER D	94	−16.982	63.218	−18.597	1	36.2	C
ATOM	5799	O	SER D	94	−15.871	62.8	−18.274	1	34.62	O
ATOM	5800	CB	SER D	94	−18.576	61.582	−19.613	1	47.3	C
ATOM	5801	OG	SER D	94	−19.526	61.895	−18.609	1	57.24	O
ATOM	5802	H	SER D	94	−15.886	62.245	−20.616	1	54.53	H
ATOM	5803	HA	SER D	94	−18.189	63.502	−20.221	1	51.4	H
ATOM	5804	HB2	SER D	94	−19.046	61.353	−20.43	1	56.75	H
ATOM	5805	HB3	SER D	94	−18.042	60.828	−19.317	1	56.75	H
ATOM	5806	HG	SER D	94	−20.025	61.234	−18.47	1	68.69	H
ATOM	5807	N	TYR D	95	−17.673	64.086	−17.866	1	33.4	N
ATOM	5808	CA	TYR D	95	−17.266	64.466	−16.52	1	33.91	C
ATOM	5809	C	TYR D	95	−17.891	63.519	−15.505	1	30.98	C
ATOM	5810	O	TYR D	95	−18.999	63.025	−15.711	1	31.07	O
ATOM	5811	CB	TYR D	95	−17.675	65.905	−16.213	1	39.04	C
ATOM	5812	CG	TYR D	95	−16.785	66.949	−16.84	1	41.85	C
ATOM	5813	CD1	TYR D	95	−15.603	67.336	−16.227	1	42.03	C
ATOM	5814	CD2	TYR D	95	−17.13	67.557	−18.04	1	50.41	C
ATOM	5815	CE1	TYR D	95	−14.785	68.293	−16.79	1	48.64	C
ATOM	5816	CE2	TYR D	95	−16.319	68.517	−18.613	1	52.83	C
ATOM	5817	CZ	TYR D	95	−15.147	68.881	−17.983	1	57.25	C
ATOM	5818	OH	TYR D	95	−14.331	69.837	−18.545	1	60.24	O
ATOM	5819	H	TYR D	95	−18.394	64.473	−18.132	1	40.08	H
ATOM	5820	HA	TYR D	95	−16.301	64.4	−16.446	1	40.69	H
ATOM	5821	HB2	TYR D	95	−18.576	66.05	−16.542	1	46.85	H
ATOM	5822	HB3	TYR D	95	−17.653	66.037	−15.252	1	46.85	H
ATOM	5823	HD1	TYR D	95	−15.356	66.941	−15.421	1	50.44	H
ATOM	5824	HD2	TYR D	95	−17.92	67.312	−18.465	1	60.5	H
ATOM	5825	HE1	TYR D	95	−13.994	68.541	−16.368	1	58.37	H
ATOM	5826	HE2	TYR D	95	−16.561	68.915	−19.418	1	63.4	H
ATOM	5827	HH	TYR D	95	−14.664	70.113	−19.265	1	72.28	H
ATOM	5828	N	CYS D	96	−17.171	63.269	−14.415	1	25.95	N
ATOM	5829	CA	CYS D	96	−17.651	62.404	−13.343	1	25	C
ATOM	5830	C	CYS D	96	−17.873	63.227	−12.08	1	26.6	C
ATOM	5831	O	CYS D	96	−17.011	64.017	−11.687	1	24.78	O
ATOM	5832	CB	CYS D	96	−16.654	61.274	−13.078	1	24.34	C
ATOM	5833	SG	CYS D	96	−17.22	60.018	−11.906	1	25.98	S
ATOM	5834	H	CYS D	96	−16.388	63.595	−14.272	1	31.14	H
ATOM	5835	HA	CYS D	96	−18.498	62.01	−13.603	1	30	H
ATOM	5836	HB2	CYS D	96	−16.465	60.826	−13.918	1	29.21	H
ATOM	5837	HB3	CYS D	96	−15.838	61.659	−12.724	1	29.21	H
ATOM	5838	N	GLY D	97	−19.032	63.042	−11.454	1	23.68	N
ATOM	5839	CA	GLY D	97	−19.358	63.738	−10.223	1	26.95	C
ATOM	5840	C	GLY D	97	−20.783	64.263	−10.206	1	29.72	C
ATOM	5841	O	GLY D	97	−21.654	63.711	−10.88	1	30.29	O
ATOM	5842	H	GLY D	97	−19.651	62.512	−11.73	1	28.42	H
ATOM	5843	HA2	GLY D	97	−19.245	63.135	−9.472	1	32.33	H
ATOM	5844	HA3	GLY D	97	−18.755	64.489	−10.108	1	32.33	H
ATOM	5845	N	PRO D	98	−21.033	65.333	−9.432	1	27.73	N
ATOM	5846	CA	PRO D	98	−20.059	66.06	−8.605	1	26.68	C
ATOM	5847	C	PRO D	98	−19.526	65.247	−7.425	1	25.52	C
ATOM	5848	O	PRO D	98	−20.262	64.465	−6.822	1	24.79	O
ATOM	5849	CB	PRO D	98	−20.855	67.272	−8.11	1	31.02	C
ATOM	5850	CG	PRO D	98	−22.272	66.852	−8.178	1	32.89	C
ATOM	5851	CD	PRO D	98	−22.37	65.945	−9.363	1	31.01	C
ATOM	5852	HA	PRO D	98	−19.315	66.363	−9.148	1	32.02	H
ATOM	5853	HB2	PRO D	98	−20.601	67.48	−7.197	1	37.23	H
ATOM	5854	HB3	PRO D	98	−20.692	68.03	−8.693	1	37.23	H
ATOM	5855	HG2	PRO D	98	−22.51	66.38	−7.366	1	39.46	H
ATOM	5856	HG3	PRO D	98	−22.837	67.632	−8.298	1	39.46	H
ATOM	5857	HD2	PRO D	98	−23.046	65.266	−9.214	1	37.21	H
ATOM	5858	HD3	PRO D	98	−22.55	66.456	−10.167	1	37.21	H
ATOM	5859	N	CYS D	99	−18.247	65.439	−7.115	1	22.53	N
ATOM	5860	CA	CYS D	99	−17.605	64.787	−5.978	1	24.42	C
ATOM	5861	C	CYS D	99	−16.595	65.739	−5.345	1	27.19	C
ATOM	5862	O	CYS D	99	−16.094	66.638	−6.017	1	26.74	O
ATOM	5863	CB	CYS D	99	−16.895	63.496	−6.407	1	28.73	C
ATOM	5864	SG	CYS D	99	−17.971	62.187	−7.066	1	27.37	S
ATOM	5865	H	CYS D	99	−17.719	65.952	−7.559	1	27.03	H
ATOM	5866	HA	CYS D	99	−18.275	64.563	−5.313	1	29.3	H
ATOM	5867	HB2	CYS D	99	−16.25	63.716	−7.097	1	34.48	H
ATOM	5868	HB3	CYS D	99	−16.432	63.131	−5.637	1	34.48	H
ATOM	5869	N	PRO D	100	−16.293	65.547	−4.051	1	23.29	N
ATOM	5870	CA	PRO D	100	−15.166	66.276	−3.458	1	27.44	C
ATOM	5871	C	PRO D	100	−13.882	66.019	−4.245	1	28.68	C
ATOM	5872	O	PRO D	100	−13.681	64.904	−4.73	1	26.75	O
ATOM	5873	CB	PRO D	100	−15.073	65.703	−2.043	1	29.15	C
ATOM	5874	CG	PRO D	100	−16.42	65.125	−1.767	1	25.98	C
ATOM	5875	CD	PRO D	100	−16.95	64.656	−3.079	1	24.13	C
ATOM	5876	HA	PRO D	100	−15.349	67.228	−3.42	1	32.93	H
ATOM	5877	HB2	PRO D	100	−14.392	65.013	−2.014	1	34.98	H
ATOM	5878	HB3	PRO D	100	−14.869	66.414	−1.415	1	34.98	H
ATOM	5879	HG2	PRO D	100	−16.333	64.382	−1.15	1	31.17	H
ATOM	5880	HG3	PRO D	100	−16.996	65.811	−1.394	1	31.17	H
ATOM	5881	HD2	PRO D	100	−16.693	63.734	−3.238	1	28.95	H
ATOM	5882	HD3	PRO D	100	−17.913	64.769	−3.115	1	28.95	H
ATOM	5883	N	LYS D	101	−13.027	67.031	−4.357	1	31.41	N
ATOM	5884	CA	LYS D	101	−11.915	66.997	−5.306	1	34.02	C
ATOM	5885	C	LYS D	101	−10.851	65.943	−4.997	1	34.04	C
ATOM	5886	O	LYS D	101	−10.078	65.57	−5.884	1	40.88	O
ATOM	5887	CB	LYS D	101	−11.254	68.377	−5.379	1	40.64	C
ATOM	5888	CG	LYS D	101	−12.15	69.458	−5.975	1	44.15	C
ATOM	5889	CD	LYS D	101	−11.383	70.749	−6.223	1	55.25	C
ATOM	5890	CE	LYS D		101	−12.306	71.866	−6.691	1	57.18	C
ATOM	5891	NZ	LYS D	101	−11.566	73.132	−6.955	1	56.55	N1+
ATOM	5892	H	LYS D		101	−13.069	67.753	−3.892	1	37.69	H
ATOM	5893	HA	LYS D	101	−12.271	66.799	−6.186	1	40.82	H
ATOM	5894	HB2	LYS D	101	−11.011	68.655	−4.482	1	48.77	H
ATOM	5895	HB3	LYS D	101	−10.459	68.314	−5.931	1	48.77	H
ATOM	5896	HG2	LYS D	101	−12.505	69.147	−6.823	1	52.98	H
ATOM	5897	HG3	LYS D		101	−12.874	69.649	−5.358	1	52.98	H
ATOM	5898	HD2	LYS D	101	−10.957	71.032	−5.399	1	66.3	H
ATOM	5899	HD3	LYS D		101	−10.716	70.598	−6.911	1	66.3	H
ATOM	5900	HE2	LYS D		101	−12.743	71.594	−7.513	1	68.62	H
ATOM	5901	HE3	LYS D		101	−12.967	72.04	−6.003	1	68.62	H
ATOM	5902	HZ1	LYS D	101	−12.132	73.763	−7.226	1	67.86	H
ATOM	5903	HZ2	LYS D	101	−11.16	73.407	−6.213	1	67.86	H
ATOM	5904	HZ3	LYS D	101	−10.955	73	−7.588	1	67.86	H
ATOM	5905	N	ASN D	102	−10.804	65.47	−3.755	1	27.12	N
ATOM	5906	CA	ASN D	102	−9.836	64.445	−3.366	1	27.98	C
ATOM	5907	C	ASN D	102	−10.503	63.098	−3.072	1	26.71	C
ATOM	5908	O	ASN D	102	−9.946	62.263	−2.36	1	25.4	O
ATOM	5909	CB	ASN D	102	−9.026	64.914	−2.15	1	30.15	C
ATOM	5910	CG	ASN D	102	−9.898	65.481	−1.045	1	36.72	C
ATOM	5911	OD1	ASN D	102	−11.12	65.332	−1.062	1	37.16	O
ATOM	5912	ND2	ASN D	102	−9.271	66.145	−0.078	1	41.06	N
ATOM	5913	H	ASN D	102	−11.322	65.725	3.118	1	32.55	H
ATOM	5914	HA	ASN D	102	−9.215	64.311	−4.099	1	33.58	H
ATOM	5915	HB2	ASN D	102	−8.535	64.16	−1.787	1	36.19	H
ATOM	5916	HB3	ASN D	102	−8.409	65.608	−2.43	1	36.19	H
ATOM	5917	HD21	ASN D	102	−9.72	66.485	0.571	1	49.28	H
ATOM	5918	HD22	ASN D	102	−8.416	66.233	−0.102	1	49.28	H
ATOM	5919	N	TRP D	103	−11.696	62.897	−3.63	1	25.27	N
ATOM	5920	CA	TRP D	103	−12.4	61.619	−3.534	1	19.72	C
ATOM	5921	C	TRP D	103	−12.378	60.891	−4.872	1	20.07	C
ATOM	5922	O	TRP D	103	−12.24	61.516	−5.927	1	20.39	O
ATOM	5923	CB	TRP D	103	−13.853	61.822	−3.094	1	22.5	C
ATOM	5924	CG	TRP D	103	−14.018	62.103	−1.636	1	21.05	C
ATOM	5925	CD1	TRP D	103	−13.247	62.919	−0.865	1	26.32	C
ATOM	5926	CD2	TRP D	103	−15.014	61.552	−0.768	1	22.01	C
ATOM	5927	NE1	TRP D	103	−13.708	62.92	0.43	1	31.25	N
ATOM	5928	CE2	TRP D	103	−14.792	62.088	0.516	1	23.75	C
ATOM	5929	CE3	TRP D	103	−16.075	60.66	−0.952	1	21.83	C
ATOM	5930	CZ2	TRP D	103	−15.589	61.759	1.611	1	26.02	C
ATOM	5931	CZ3	TRP D	103	−16.868	60.336	0.136	1	24.01	C
ATOM	5932	CH2	TRP D	103	−16.62	60.884	1.401	1	22.41	C
ATOM	5933	H	TRP D	103	−12.124	63.494	−4.077	1	30.33	H
ATOM	5934	HA	TRP D	103	−11.959	61.06	−2.876	1	23.66	H
ATOM	5935	HB2	TRP D	103	−14.225	62.572	−3.583	1	27	H
ATOM	5936	HB3	TRP D	103	−14.355	61.017	−3.298	1	27	H
ATOM	5937	HD1	TRP D	103	−12.52	63.412	−1.172	1	31.59	H
ATOM	5938	HE1	TRP D	103	−13.369	63.369	1.081	1	37.5	H
ATOM	5939	HE3	TRP D	103	−16.245	60.292	1.789	1	26.2	H
ATOM	5940	HZ2	TRP D	103	−15.427	62.122	2.452	1	31.22	H
ATOM	5941	HZ3	TRP D	103	−17.577	59.744	0.025	1	28.82	H
ATOM	5942	HH2	TRP D	103	−17.169	60.649	2.114	1	26.9	H
ATOM	5943	N	ILE D	104	−12.524	59.571	−4.821	1	16.86	N
ATOM	5944	CA	ILE D	104	−12.597	58.755	−6.027	1	17.78	C
ATOM	5945	C	ILE D	104	−13.993	58.831	−6.627	1	18.2	C
ATOM	5946	O	ILE D	104	−14.975	58.549	−5.944	1	18.57	O
ATOM	5947	CB	ILE D	104	−12.255	57.281	−5.735	1	20.02	C
ATOM	5948	CG1	ILE D	104	−10.857	57.168	−5.119	1	20.67	C
ATOM	5949	CG2	ILE D	104	−12.338	56.446	−7.015	1	19.79	C
ATOM	5950	CD1	ILE D	104	−10.571	55.825	−4.483	1	17.1	C
ATOM	5951	H	ILE D	104	−12.585	59.12	−4.092	1	20.23	H
ATOM	5952	HA	ILE D	104	−11.965	59.091	−6.681	1	21.34	H
ATOM	5953	HB	ILE D	104	−12.901	56.935	−5.099	1	24.02	H
ATOM	5954	HG12	ILE D	104	−10.197	57.313	−5.815	1	24.8	H
ATOM	5955	HG13	ILE D	104	−10.763	57.847	−4.432	1	24.8	H
ATOM	5956	HG21	ILE D	104	−12.12	55.525	−6.805	1	23.75	H
ATOM	5957	HG22	ILE D	104	−13.24	56.5	−7.368	1	23.75	H
ATOM	5958	HG23	ILE D	104	−11.707	56.798	−7.662	1	23.75	H
ATOM	5959	HD11	ILE D	104	−9.673	55.834	−4.118	1	20.52	H
ATOM	5960	HD12	ILE D	104	−11.215	55.668	−3.774	1	20.52	H
ATOM	5961	HD13	ILE D	104	−10.648	55.134	−5.159	1	20.52	H
ATOM	5962	N	CYS D	105	−14.076	59.199	−7.902	1	17.45	N
ATOM	5963	CA	CYS D	105	−15.354	59.239	−8.602	1	17.74	C
ATOM	5964	C	CYS D	105	−15.465	58.067	−9.573	1	21.3	C
ATOM	5965	O	CYS D	105	−14.56	57.821	−10.371	1	19.85	O
ATOM	5966	CB	CYS D	105	−15.524	60.563	−9.345	1	20.49	C
ATOM	5967	SG	CYS D	105	−17.186	60.797	−10.022	1	29.47	S
ATOM	5968	H	CYS D	105	−13.404	59.431	−8.385	1	20.94	H
ATOM	5969	HA	CYS D	105	−16.073	59.163	−7.955	1	21.29	H
ATOM	5970	HB2	CYS D	105	−15.347	61.293	−8.731	1	24.59	H
ATOM	5971	HB3	CYS D	105	−14.895	60.592	−10.083	1	24.59	H
ATOM	5972	N	TYR D		106	−16.577	57.343	−9.481	1	17.44	N
ATOM	5973	CA	TYR D	106	−16.858	56.216	−10.365	1	18.5	C
ATOM	5974	C	TYR D	106	−18.354	56.134	−10.632	1	19.85	C
ATOM	5975	O	TYR D	106	−19.139	55.879	−9.718	1	18.05	O
ATOM	5976	CB	TYR D	106	−16.362	54.902	−9.755	1	15.27	C
ATOM	5977	CG	TYR D	106	−16.488	53.707	−10.675	1	17.55	C
ATOM	5978	CD1	TYR D	106	−15.878	53.702	−11.922	1	20.29	C
ATOM	5979	CD2	TYR D	106	−17.202	52.577	−10.293	1	20.08	C
ATOM	5980	CE1	TYR D	106	−15.981	52.613	−12.768	1	20.5	C
ATOM	5981	CE2	TYR D	106	−17.309	51.476	−11.136	1	18.23	C
ATOM	5982	CZ	TYR D	106	−16.692	51.502	−12.373	1	22.08	C
ATOM	5983	OH	TYR D	106	−16.785	50.418	−13.224	1	18.81	O
ATOM	5984	H	TYR D	106	−17.196	57.488	−8.902	1	20.92	H
ATOM	5985	HA	TYR D	106	−16.403	56.351	−11.211	1	22.2	H
ATOM	5986	HB2	TYR D	106	−15.425	55	−9.524	1	18.33	H
ATOM	5987	HB3	TYR D	106	−16.879	54.715	−8.956	1	18.33	H
ATOM	5988	HD1	TYR D	106	−15.394	54.448	−12.195	1	24.35	H
ATOM	5989	HD2	TYR D	106	−17.616	52.557	−9.46	1	24.1	H
ATOM	5990	HE1	TYR D	106	−15.565	52.629	−13.6	1	24.6	H
ATOM	5991	HE2	TYR D	106	−17.79	50.727	−10.869	1	21.87	H
ATOM	5992	HH	TYR D	106	−17.243	49.811	−12.867	1	22.58	H
ATOM	5993	N	LYS D		107	−18.732	56.351	−11.888	1	16.29	N
ATOM	5994	CA	LYS D	107	−20.132	56.364	−12.294	1	20.57	C
ATOM	5995	C	LYS D	107	−20.916	57.33	−11.404	1	24.05	C
ATOM	5996	O	LYS D		107	−21.998	57.015	−10.907	1	17.53	O
ATOM	5997	CB	LYS D	107	−20.708	54.947	−12.249	1	20.83	C
ATOM	5998	CG	LYS D	107	−19.963	53.987	−13.184	1	20.22	C
ATOM	5999	CD	LYS D	107	−20.505	52.566	−13.145	1	20.35	C
ATOM	6000	CE	LYS D		107	−19.817	51.694	−14.198	1	23.07	C
ATOM	6001	NZ	LYS D	107	−20.217	50.259	−14.138	1	21	N1+
ATOM	6002	H	LYS D	107	−18.185	56.495	−12.536	1	19.55	H
ATOM	6003	HA	LYS D		107	−20.193	56.682	−13.208	1	24.68	H
ATOM	6004	HB2	LYS D	107	−20.637	54.604	−11.344	1	24.99	H
ATOM	6005	HB3	LYS D	107	−21.638	54.974	−12.523	1	24.99	H
ATOM	6006	HG2	LYS D	107	−20.041	54.311	−14.094	1	24.26	H
ATOM	6007	HG3	LYS D		107	−19.029	53.957	−12.923	1	24.26	H
ATOM	6008	HD2	LYS D	107	−20.338	52.18	−12.271	1	24.42	H
ATOM	6009	HD3	LYS D	107	−21.457	52.579	−13.332	1	24.42	H
ATOM	6010	HE2	LYS D		107	−20.045	52.029	−15.08	1	27.69	H
ATOM	6011	HE3	LYS D		107	−18.857	51.741	−14.065	1	27.69	H
ATOM	6012	HZ1	LYS D	107	−21.095	50.182	−14.267	1	25.2	H
ATOM	6013	HZ2	LYS D		107	−19.791	49.797	−14.768	1	25.2	H
ATOM	6014	HZ3	LYS D		107	−20.011	49.919	−13.341	1	25.2	H
ATOM	6015	N	ASN D	108	−20.318	58.503	−11.205	1	23.09	N
ATOM	6016	CA	ASN D	108	−20.912	59.622	−10.473	1	24.38	C
ATOM	6017	C	ASN D	108	−21.096	59.378	−8.976	1	22.29	C
ATOM	6018	O	ASN D	108	−21.565	60.261	−8.262	1	28.01	O
ATOM	6019	CB	ASN D	108	−22.253	60.012	−11.103	1	25.1	C
ATOM	6020	CG	ASN D	108	−22.084	60.642	−12.471	1	28.43	C
ATOM	6021	OD1	ASN D	108	−21.044	61.229	−12.769	1	25.66	O
ATOM	6022	ND2	ASN D	108	−23.107	60.529	−13.31	1	30.87	N
ATOM	6023	H	ASN D	108	−19.53	58.682	−11.5	1	27.71	H
ATOM	6024	HA	ASN D	108	−20.321	60.386	−10.565	1	29.25	H
ATOM	6025	HB2	ASN D	108	−22.8	59.217	−11.203	1	30.12	H
ATOM	6026	HB3	ASN D	108	−22.698	60.654	−10.529	1	30.12	H
ATOM	6027	HD21	ASN D	108	−23.057	60.871	−14.098	1	37.04	H
ATOM	6028	HD22	ASN D	108	−23.82	60.115	−13.066	1	37.04	H
ATOM	6029	N	ASN D	109	−20.704	58.205	−8.494	1	21.22	N
ATOM	6030	CA	ASN D	109	−20.646	57.967	−7.056	1	19.34	C
ATOM	6031	C	ASN D	109	−19.262	58.34	−6.533	1	19.61	C
ATOM	6032	O	ASN D	109	−18.267	58.162	−7.232	1	16.71	O
ATOM	6033	CB	ASN D	109	−20.973	56.512	−6.733	1	19.32	C
ATOM	6034	CG	ASN D	109	−22.421	56.167	−7.013	1	25.66	C
ATOM	6035	OD1	ASN D	109	−23.322	56.973	−6.77	1	19.34	O
ATOM	6036	ND2	ASN D	109	−22.652	54.969	7.533	1	19.02	N
ATOM	6037	H	ASN D	109	−20.467	57.532	−8.974	1	25.47	H
ATOM	6038	HA	ASN D	109	−21.3	58.53	−6.613	1	23.2	H
ATOM	6039	HB2	ASN D	109	−20.415	55.934	−7.278	1	23.19	H
ATOM	6040	HB3	ASN D	109	−20.801	56.35	−5.792	1	23.19	H
ATOM	6041	HD21	ASN D	109	−23.457	54.725	−7.71	1	22.82	H
ATOM	6042	HD22	ASN D	109	−21.996	54.436	−7.693	1	22.82	H
ATOM	6043	N	CYS D	110	−19.204	58.867	−5.312	1	17.46	N
ATOM	6044	CA	CYS D	110	−17.941	59.308	−4.726	1	16.88	C
ATOM	6045	C	CYS D	110	−17.547	58.402	−3.573	1	19.16	C
ATOM	6046	O	CYS D	110	−18.374	58.079	−2.725	1	17.29	O
ATOM	6047	CB	CYS D	110	−18.047	60.751	−4.237	1	22.6	C
ATOM	6048	SG	CYS D	110	−18.972	61.837	−5.338	1	23.11	S
ATOM	6049	H	CYS D	110	−19.886	58.981	−4.801	1	20.95	H
ATOM	6050	HA	CYS D	110	−17.244	59.265	−5.399	1	20.25	H
ATOM	6051	HB2	CYS D	110	−18.493	60.756	−3.375	1	27.12	H
ATOM	6052	HB3	CYS D	110	−17.153	61.116	−4.145	1	27.12	H
ATOM	6053	N	TYR D	111	−16.28	58.001	−3.545	1	18.03	N
ATOM	6054	CA	TYR D	111	−15.768	57.132	−2.489	1	17.44	C
ATOM	6055	C	TYR D	111	−14.471	57.677	−1.92	1	15.34	C
ATOM	6056	O	TYR D	111	−13.731	58.388	−2.6	1	20.2	O
ATOM	6057	CB	TYR D	111	−15.515	55.718	−3.016	1	18.77	C
ATOM	6058	CG	TYR D	111	−16.678	55.089	−3.737	1	20.6	C
ATOM	6059	CD1	TYR D	111	−16.879	55.308	−5.09	1	15.51	C
ATOM	6060	CD2	TYR D	111	−17.561	54.251	−3.07	1	20.76	C
ATOM	6061	CE1	TYR D	111	−17.936	54.723	−5.757	1	18.59	C
ATOM	6062	CE2	TYR D	111	−18.625	53.664	−3.728	1	17.85	C
ATOM	6063	CZ	TYR D	111	−18.806	53.903	−5.071	1	18.9	C
ATOM	6064	OH	TYR D	111	−19.868	53.323	−5.732	1	19.85	O
ATOM	6065	H	TYR D	111	−15.691	58.22	4.132	1	21.63	H
ATOM	6066	HA	TYR D	111	−16.418	57.08	−1.772	1	20.92	H
ATOM	6067	HB2	TYR D	111	−14.769	55.748	−3.635	1	22.52	H
ATOM	6068	HB3	TYR D	111	−15.291	55.145	−2.266	1	22.52	H
ATOM	6069	HD1	TYR D	111	−16.294	55.862	−5.556	1	18.61	H
ATOM	6070	HD2	TYR D	111	−17.44	54.089	−2.162	1	24.91	H
ATOM	6071	HE1	TYR D	111	−18.064	54.885	6.664	1	22.3	H
ATOM	6072	HE2	TYR D	111	−19.212	53.11	−3.267	1	21.42	H
ATOM	6073	HH	TYR D	111	−19.863	53.553	−6.54	1	23.82	H
ATOM	6074	N	GLN D	112	−14.19	57.329	−0.673	1	17.91	N
ATOM	6075	CA	GLN D	112	−12.866	57.552	−0.119	1	20.98	C
ATOM	6076	C	GLN D	112	−12.549	56.483	0.914	1	18.4	C
ATOM	6077	O	GLN D	112	−13.417	56.045	1.668	1	17.57	O
ATOM	6078	CB	GLN D	112	−12.75	58.949	0.496	1	23.03	C
ATOM	6079	CG	GLN D	112	−11.326	59.331	0.905	1	24.86	C
ATOM	6080	CD	GLN D	112	−10.317	59.175	−0.225	1	29.43	C
ATOM	6081	OE1	GLN D	112	−9.797	58.083	−0.469	1	32.59	O
ATOM	6082	NE2	GLN D	112	−10.033	60.27	−0.92	1	35.19	N
ATOM	6083	H	GLN D	112	−14.747	56.965	−0.128	1	21.49	H
ATOM	6084	HA	GLN D	112	−12.211	57.483	−0.831	1	25.18	H
ATOM	6085	HB2	GLN D	112	−13.057	59.602	−0.152	1	27.63	H
ATOM	6086	HB3	GLN D	112	−13.306	58.987	1.29	1	27.63	H
ATOM	6087	HG2	GLN D	112	−11.318	60.259	1.187	1	29.83	H
ATOM	6088	HG3	GLN D	112	−11.045	58.76	1.637	1	29.83	H
ATOM	6089	HE21	GLN D	112	−9.469	60.234	−1.568	1	42.23	H
ATOM	6090	HE22	GLN D	112	−10.414	61.015	−0.721	1	42.23	H
ATOM	6091	N	PHE D	113	−11.293	56.059	0.921	1	15.24	N
ATOM	6092	CA	PHE D	113	−10.808	55.082	1.878	1	19.47	C
ATOM	6093	C	PHE D	113	−10.013	55.796	2.963	1	22.57	C
ATOM	6094	O	PHE D	113	−9.202	56.678	2.676	1	28.44	O
ATOM	6095	CB	PHE D	113	−9.955	54.026	1.172	1	25.43	C
ATOM	6096	CG	PHE D	113	−10.73	53.179	0.198	1	22.13	C
ATOM	6097	CD1	PHE D	113	−11.227	53.727	−0.976	1	29.41	C
ATOM	6098	CD2	PHE D	113	−10.953	51.836	0.45	1	23.89	C
ATOM	6099	CE1	PHE D	113	−11.94	52.951	−1.877	1	30.31	C
ATOM	6100	CE2	PHE D	113	−11.666	51.054	−0.447	1	21.37	C
ATOM	6101	CZ	PHE D	113	−12.16	51.613	−1.61	1	23.83	C
ATOM	6102	H	PHE D	113	−10.692	56.33	0.369	1	18.29	H
ATOM	6103	HA	PHE D	113	−11.562	54.637	2.294	1	23.37	H
ATOM	6104	HB2	PHE D	113	−9.247	54.472	0.681	1	30.51	H
ATOM	6105	HB3	PHE D	113	−9.571	53.436	1.839	1	30.51	H
ATOM	6106	HD1	PHE D	113	−11.084	54.627	−1.159	1	35.29	H
ATOM	6107	HD2	PHE D	113	−10.625	51.455	1.232	1	28.66	H
ATOM	6108	HE1	PHE D	113	−12.27	53.33	−2.659	1	36.37	H
ATOM	6109	HE2	PHE D	113	−11.812	50.154	−0.265	1	25.65	H
ATOM	6110	HZ	PHE D	113	−12.637	51.089	−2.213	1	28.6	H
ATOM	6111	N	PHE D	114	−10.275	55.42	4.209	1	21.22	N
ATOM	6112	CA	PHE D	114	−9.633	56.027	5.368	1	22.84	C
ATOM	6113	C	PHE D	114	−8.84	54.967	6.111	1	25.57	C
ATOM	6114	O	PHE D	114	−9.409	53.987	6.59	1	20.97	O
ATOM	6115	CB	PHE D	114	−10.682	56.665	6.28	1	25.74	C
ATOM	6116	CG	PHE D	114	−11.434	57.787	5.629	1	22.57	C
ATOM	6117	CD1	PHE D	114	−12.523	57.53	4.817	1	23.79	C
ATOM	6118	CD2	PHE D	114	−11.041	59.102	5.819	1	30.88	C
ATOM	6119	CE1	PHE D	114	−13.208	58.562	4.209	1	26.61	C
ATOM	6120	CE2	PHE D	114	−11.723	60.139	5.214	1	23.44	C
ATOM	6121	CZ	PHE D	114	−12.809	59.869	4.409	1	28.06	C
ATOM	6122	H	PHE D	114	−10.835	54.801	4.413	1	25.46	H
ATOM	6123	HA	PHE D	114	−9.02	56.719	5.073	1	27.4	H
ATOM	6124	HB2	PHE D	114	−11.325	55.987	6.54	1	30.89	H
ATOM	6125	HB3	PHE D	114	−10.24	57.019	7.067	1	30.89	H
ATOM	6126	HD1	PHE D	114	−12.796	56.652	4.678	1	28.55	H
ATOM	6127	HD2	PHE D	114	−10.308	59.288	6.361	1	37.05	H
ATOM	6128	HE1	PHE D	114	−13.941	58.378	3.667	1	31.94	H
ATOM	6129	HE2	PHE D	114	−11.451	61.018	5.351	1	28.13	H
ATOM	6130	HZ	PHE D	114	−13.271	60.565	4.001	1	33.67	H
ATOM	6131	N	ASP D	115	−7.526	55.161	6.199	1	23.12	N
ATOM	6132	CA	ASP D	115	−6.645	54.131	6.737	1	26.22	C
ATOM	6133	C	ASP D	115	−6.365	54.317	8.228	1	30.31	C
ATOM	6134	O	ASP D	115	−5.656	53.516	8.831	1	25.41	O
ATOM	6135	CB	ASP D	115	−5.328	54.096	5.957	1	27.72	C
ATOM	6136	CG	ASP D	115	−4.615	55.436	5.94	1	34.76	C
ATOM	6137	OD1	ASP D	115	−5.1	56.389	6.587	1	33.82	O
ATOM	6138	OD2	ASP D	115	−3.558	55.53	5.282	1	32.71	O1−
ATOM	6139	H	ASP D	115	−7.122	55.879	5.954	1	27.74	H
ATOM	6140	HA	ASP D	115	−7.075	53.269	6.626	1	31.46	H
ATOM	6141	HB2	ASP D	115	−4.735	53.447	6.367	1	33.26	H
ATOM	6142	HB3	ASP D	115	−5.512	53.843	5.039	1	33.26	H
ATOM	6143	N	GLU D	116	−6.92	55.373	8.817	1	29.51	N
ATOM	6144	CA	GLU D	116	−6.821	55.578	10.259	1	35.02	C
ATOM	6145	C	GLU D	116	−7.96	54.814	10.921	1	33.34	C
ATOM	6146	O	GLU D	116	−9.096	55.282	10.94	1	33.54	O
ATOM	6147	CB	GLU D	116	−6.88	57.067	10.624	1	38.38	C
ATOM	6148	CG	GLU D	116	−5.921	57.96	9.836	1	42.91	C
ATOM	6149	CD	GLU D	116	−6.444	58.351	8.458	1	44.87	C
ATOM	6150	OE1	GLU D	116	−7.627	58.078	8.155	1	38.52	O
ATOM	6151	OE2	GLU D	116	−5.664	58.934	7.673	1	52.44	O1−
ATOM	6152	H	GLU D	116	−7.36	55.986	8.404	1	35.41	H
ATOM	6153	HA	GLU D	116	−5.98	55.216	10.58	1	42.03	H
ATOM	6154	HB2	GLU D	116	−7.781	57.389	10.462	1	46.06	H
ATOM	6155	HB3	GLU D	116	−6.665	57.163	11.565	1	46.06	H
ATOM	6156	HG2	GLU D	116	−5.768	58.775	10.338	1	51.49	H
ATOM	6157	HG3	GLU D	116	−5.083	57.487	9.712	1	51.49	H
ATOM	6158	N	SER D	117	−7.65	53.636	11.457	1	30.25	N
ATOM	6159	CA	SER D	117	−8.674	52.697	11.907	1	27.86	C
ATOM	6160	C	SER D	117	−9.509	53.219	13.077	1	33.38	C
ATOM	6161	O	SER D	117	−8.988	53.81	14.022	1	30.47	O
ATOM	6162	CB	SER D	117	−8.028	51.365	12.297	1	31.01	C
ATOM	6163	OG	SER D	117	−7.15	51.529	13.392	1	34.1	O
ATOM	6164	H	SER D	117	−6.845	53.355	11.571	1	36.3	H
ATOM	6165	HA	SER D	117	−9.279	52.525	11.169	1	33.44	H
ATOM	6166	HB2	SER D	117	−8.725	50.737	12.543	1	37.21	H
ATOM	6167	HB3	SER D	117	−7.527	51.024	11.539	1	37.21	H
ATOM	6168	HG	SER D	117	−6.803	50.792	13.595	1	40.92	H
ATOM	6169	N	LYS D	118	−10.814	52.976	12.992	1	27.74	N
ATOM	6170	CA	LYS D	118	−11.771	53.385	14.015	1	27.96	C
ATOM	6171	C	LYS D	118	−12.805	52.284	14.202	1	31.8	C
ATOM	6172	O	LYS D	118	−12.946	51.409	13.343	1	27.27	O
ATOM	6173	CB	LYS D	118	−12.464	54.689	13.619	1	25.67	C
ATOM	6174	CG	LYS D	118	−11.533	55.875	13.44	1	29.25	C
ATOM	6175	CD	LYS D	118	−12.293	57.075	12.904	1	36.12	C
ATOM	6176	CE	LYS D	118	−11.416	58.312	12.827	1	36.2	C
ATOM	6177	NZ	LYS D	118	−10.988	58.767	14.175	1	46.64	N1+
ATOM	6178	H	LYS D	118	−11.179	52.564	12.332	1	33.29	H
ATOM	6179	HA	LYS D	118	−11.309	53.523	14.856	1	33.55	H
ATOM	6180	HB2	LYS D	118	−12.928	54.55	12.778	1	30.81	H
ATOM	6181	HB3	LYS D	118	−13.105	54.921	14.31	1	30.81	H
ATOM	6182	HG2	LYS D	118	−11.146	56.114	14.297	1	35.1	H
ATOM	6183	HG3	LYS D	118	−10.836	55.645	12.806	1	35.1	H
ATOM	6184	HD2	LYS D	118	−12.615	56.876	12.011	1	43.34	H
ATOM	6185	HD3	LYS D	118	−13.039	57.269	13.493	1	43.34	H
ATOM	6186	HE2	LYS D	118	−10.621	58.108	12.31	1	43.44	H
ATOM	6187	HE3	LYS D	118	−11.914	59.031	12.408	1	43.44	H
ATOM	6188	HZ1	LYS D	118	−10.477	59.492	14.103	1	55.96	H
ATOM	6189	HZ2	LYS D	118	−11.701	58.965	14.67	1	55.96	H
ATOM	6190	HZ3	LYS D	118	−10.524	58.125	14.58	1	55.96	H
ATOM	6191	N	ASN D	119	−13.531	52.314	15.316	1	28.46	N
ATOM	6192	CA	ASN D	119	−14.632	51.378	15.495	1	27.04	C
ATOM	6193	C	ASN D	119	−15.773	51.811	14.585	1	24.03	C
ATOM	6194	O	ASN D	119	−15.713	52.884	13.985	1	24.95	O
ATOM	6195	CB	ASN D	119	−15.068	51.301	16.964	1	27.48	C
ATOM	6196	CG	ASN D	119	−15.649	52.6	17.483	1	26.83	C
ATOM	6197	OD1	ASN D	119	−16.565	53.173	16.895	1	25.34	O
ATOM	6198	ND2	ASN D	119	−15.119	53.069	18.606	1	37.21	N
ATOM	6199	H	ASN D	119	−13.408	52.858	15.971	1	34.15	H
ATOM	6200	HA	ASN D	119	−14.345	50.494	15.22	1	32.45	H
ATOM	6201	HB2	ASN D	119	−15.747	50.613	17.054	1	32.97	H
ATOM	6202	HB3	ASN D	119	−14.298	51.079	17.51	1	32.97	H
ATOM	6203	HD21	ASN D	119	−15.411	53.803	18.945	1	44.65	H
ATOM	6204	HD22	ASN D	119	−14.484	52.638	18.994	1	44.65	H
ATOM	6205	N	TRP D	120	−16.807	50.986	14.472	1	21.37	N
ATOM	6206	CA	TRP D	120	−17.855	51.238	13.492	1	24.98	C
ATOM	6207	C	TRP D	120	−18.589	52.545	13.77	1	24.15	C
ATOM	6208	O	TRP D	120	−18.945	53.274	12.844	1	19.58	O
ATOM	6209	CB	TRP D	120	−18.855	50.083	13.46	1	21.6	C
ATOM	6210	CG	TRP D	120	−19.879	50.242	12.386	1	23.54	C
ATOM	6211	CD1	TRP D	120	−19.797	49.787	11.102	1	24.11	C
ATOM	6212	CD2	TRP D	120	−21.137	50.917	12.493	1	26.63	C
ATOM	6213	NE1	TRP D	120	−20.927	50.135	10.404	1	25.43	N
ATOM	6214	CE2	TRP D	120	−21.766	50.828	11.236	1	27.74	C
ATOM	6215	CE3	TRP D	120	−21.793	51.587	13.531	1	30.26	C
ATOM	6216	CZ2	TRP D	120	−23.02	51.379	10.989	1	28.23	C
ATOM	6217	CZ3	TRP D	120	−23.036	52.136	13.283	1	28.53	C
ATOM	6218	CH2	TRP D	120	−23.637	52.03	12.022	1	29.49	C
ATOM	6219	H	TRP D	120	−16.924	50.278	14.947	1	25.65	H
ATOM	6220	HA	TRP D	120	−17.452	51.305	12.612	1	29.98	H
ATOM	6221	HB2	TRP D	120	−18.377	49.255	13.3	1	25.92	H
ATOM	6222	HB3	TRP D	120	−19.317	50.041	14.312	1	25.92	H
ATOM	6223	HD1	TRP D	120	−19.079	49.312	10.75	1	28.93	H
ATOM	6224	HE1	TRP D	120	−21.084	49.945	9.58	1	30.52	H
ATOM	6225	HE3	TRP D	120	−21.4	51.661	14.37	1	36.31	H
ATOM	6226	HZ2	TRP D	120	−23.421	51.312	10.153	1	33.87	H
ATOM	6227	HZ3	TRP D	120	−23.482	52.583	13.965	1	34.24	H
ATOM	6228	HH2	TRP D	120	−24.475	52.408	11.885	1	35.38	H
ATOM	6229	N	TYR D	121	−18.808	52.839	15.047	1	27.37	N
ATOM	6230	CA	TYR D	121	−19.558	54.028	15.438	1	29.38	C
ATOM	6231	C	TYR D	121	−18.799	55.295	15.065	1	22.01	C
ATOM	6232	O0	TYR D	121	−19.365	56.214	14.481	1	23.03	O
ATOM	6233	CB	TYR D	121	−19.857	54.001	16.939	1	32.74	C
ATOM	6234	CG	TYR D	121	−20.587	52.751	17.378	1	29.99	C
ATOM	6235	CD1	TYR D	121	−21.946	52.598	17.144	1	35.21	C
ATOM	6236	CD2	TYR D	121	−19.911	51.718	18.016	1	32.98	C
ATOM	6237	CE1	TYR D	121	−22.616	51.452	17.538	1	36.69	C
ATOM	6238	CE2	TYR D	121	−20.571	50.569	18.414	1	36.17	C
ATOM	6239	CZ	TYR D	121	−21.922	50.442	18.172	1	40.29	C
ATOM	6240	OH	TYR D	121	−22.582	49.3	18.566	1	49.6	O
ATOM	6241	H	TYR D	121	−18.531	52.365	15.709	1	32.84	H
ATOM	6242	HA	TYR D	121	−20.405	54.036	14.964	1	35.25	H
ATOM	6243	HB2	TYR D	121	−19.02	54.046	17.428	1	39.29	H
ATOM	6244	HB3	TYR D	121	−20.412	54.765	17.163	1	39.29	H
ATOM	6245	HD1	TYR D	121	−22.416	53.277	16.716	1	42.26	H
ATOM	6246	HD2	TYR D	121	−19	51.801	18.18	1	39.57	H
ATOM	6247	HE1	TYR D	121	−23.527	51.364	17.376	1	44.02	H
ATOM	6248	HE2	TYR D	121	−20.106	49.887	18.842	1	43.4	H
ATOM	6249	HH	TYR D	121	−22.045	48.771	18.937	1	59.52	H
ATOM	6250	N	GLU D	122	−17.513	55.332	15.395	1	23.53	N
ATOM	6251	CA	GLU D	122	−16.664	56.463	15.044	1	26.93	C
ATOM	6252	C	GLU D	122	−16.509	56.579	13.53	1	25.72	C
ATOM	6253	O	GLU D	122	−16.406	57.68	12.991	1	23.66	O
ATOM	6254	CB	GLU D	122	−15.294	56.318	15.702	1	31.25	C
ATOM	6255	CG	GLU D	122	−15.338	56.331	17.223	1	35.27	C
ATOM	6256	CD	GLU D	122	−14.056	55.821	17.855	1	43.03	C
ATOM	6257	OE1	GLU D	122	−13.27	55.135	17.162	1	42.6	O
ATOM	6258	OE2	GLU D	122	−13.837	56.104	19.051	1	53.83	O1−
ATOM	6259	H	GLU D	122	−17.105	54.71	15.826	1	28.23	H
ATOM	6260	HA	GLU D	122	−17.071	57.281	15.37	1	32.32	H
ATOM	6261	HB2	GLU D	122	−14.902	55.475	15.424	1	37.5	H
ATOM	6262	HB3	GLU D	122	−14.73	57.053	15.415	1	37.5	H
ATOM	6263	HG2	GLU D	122	−15.48	57.241	17.526	1	42.33	H
ATOM	6264	HG3	GLU D	122	−16.066	55.764	17.522	1	42.33	H
ATOM	6265	N	SER D	123	−16.486	55.436	12.848	1	21.52	N
ATOM	6266	CA	SER D	123	−16.412	55.419	11.391	1	23.2	C
ATOM	6267	C	SER D	123	−17.68	56.03	10.804	1	23.42	C
ATOM	6268	O	SER D	123	−17.62	56.862	9.898	1	20.31	O
ATOM	6269	CB	SER D	123	−16.216	53.993	10.871	1	21.62	C
ATOM	6270	OG	SER D	123	−14.982	53.454	11.306	1	19.63	O
ATOM	6271	H	SER D	123	−16.512	54.655	13.208	1	25.82	H
ATOM	6272	HA	SER D	123	−15.656	55.954	11.103	1	27.84	H
ATOM	6273	HB2	SER D	123	−16.938	53.435	11.202	1	25.94	H
ATOM	6274	HB3	SER D	123	−16.229	54.007	9.901	1	25.94	H
ATOM	6275	HG	SER D	123	−14.957	53.434	12.146	1	23.55	H
ATOM	6276	N	GLN D	124	−18.827	55.611	11.331	1	20.37	N
ATOM	6277	CA	GLN D	124	−20.107	56.17	10.922	1	24.01	C
ATOM	6278	C	GLN D	124	−20.123	57.683	11.103	1	25.04	C
ATOM	6279	O	GLN D	124	−20.549	58.42	10.214	1	21.92	O
ATOM	6280	CB	GLN D	124	−21.238	55.534	11.725	1	28.29	C
ATOM	6281	CG	GLN D	124	−22.605	56.135	11.471	1	32.29	C
ATOM	6282	CD	GLN D	124	−23.667	55.497	12.338	1	34.18	C
ATOM	6283	OE1	GLN D	124	−23.49	55.356	13.549	1	37.41	O
ATOM	6284	NE2	GLN D	124	−24.773	55.089	11.722	1	37.93	N
ATOM	6285	H	GLN D	124	−18.888	55	11.933	1	24.45	H
ATOM	6286	HA	GLN D	124	−20.255	55.975	9.983	1	28.81	H
ATOM	6287	HB2	GLN D	124	−21.284	54.591	11.501	1	33.95	H
ATOM	6288	HB3	GLN D	124	−21.042	55.636	12.669	1	33.95	H
ATOM	6289	HG2	GLN D	124	−22.579	57.083	11.672	1	38.75	H
ATOM	6290	HG3	GLN D	124	−22.848	55.995	10.543	1	38.75	H
ATOM	6291	HE21	GLN D	124	−25.405	54.72	12.174	1	45.51	H
ATOM	6292	HE22	GLN D	124	−24.855	55.194	10.873	1	45.51	H
ATOM	6293	N	ALA D	125	−19.652	58.135	12.26	1	25.98	N
ATOM	6294	CA	ALA D	125	−19.64	59.555	12.584	1	27.07	C
ATOM	6295	C	ALA D	125	−18.721	60.311	11.636	1	24.27	C
ATOM	6296	O	ALA D	125	−19.057	61.397	11.168	1	27.08	O
ATOM	6297	CB	ALA D	125	−19.207	59.766	14.027	1	26.32	C
ATOM	6298	H	ALA D	125	−19.331	57.633	12.88	1	31.18	H
ATOM	6299	HA	ALA D	125	−20.537	59.912	12.483	1	32.48	H
ATOM	6300	HB1	ALA D	125	−19.206	60.716	14.221	1	31.59	H
ATOM	6301	HB2	ALA D	125	−19.830	59.309	14.613		131.59	H
ATOM	6302	HB3	ALA D	125	−18.315	59.403	14.144		131.59	H
ATOM	6303	N	SER D	126	−17.562	59.727	11.351		125.39	N
ATOM	6304	CA	SER D	126	−16.606	60.338	10.437		125.90	C
ATOM	6305	C	SER D	126	−17.233	60.587	9.066		121.76	C
ATOM	6306	O	SER D	126	−17.156	61.693	8.535		120.77	O
ATOM	6307	CB	SER D	126	−15.363	59.460	10.298		124.59	C
ATOM	6308	OG	SER D	126	−14.403	60.072	9.456		123.90	O
ATOM	6309	H	SER D	126	−17.305	58.973	11.676		130.47	H
ATOM	6310	HA	SER D	126	−16.328	61.195	10.798		131.08	H
ATOM	6311	HB2	SER D	126	−14.973	59.325	11.175		129.51	H
ATOM	6312	HB3	SER D	126	−15.621	58.607	9.915		129.51	H
ATOM	6313	HG	SER D	126	−13.725	59.580	9.388		128.69	H
ATOM	6314	N	CYS D	127	−17.866	59.564	8.501		122.12	N
ATOM	6315	CA	CYS D	127	−18.500	59.692	7.192		122.37	C
ATOM	6316	C	CYS D	127	−19.619	60.731	7.206		123.64	C
ATOM	6317	O	CYS D	127	−19.765	61.513	6.260		123.85	O
ATOM	6318	CB	CYS D	127	−19.053	58.341	6.731		123.71	C
ATOM	6319	SG	CYS D	127	−17.786	57.091	6.427		120.25	S
ATOM	6320	H	CYS D	127	−17.943	58.784	8.855		126.54	H
ATOM	6321	HA	CYS D	127	−17.834	59.978	6.548		126.84	H
ATOM	6322	HB2	CYS D	127	−19.648	57.998	7.415		128.45	H
ATOM	6323	HB3	CYS D	127	−19.544	58.471	5.905		128.45	H
ATOM	6324	N	MET D	128	−20.406	60.737	8.277		124.97	N
ATOM	6325	CA	MET D	128	−21.524	61.668	8.398		126.23	C
ATOM	6326	C	MET D	128	−21.036	63.111	8.394		126.46	C
ATOM	6327	O	MET D	128	−21.642	63.975	7.764		129.60	O
ATOM	6328	CB	MET D	128	−22.322	61.394	9.673		127.84	C
ATOM	6329	CG	MET D	128	−23.246	60.187	9.582		142.42	C
ATOM	6330	SD	MET D	128	−24.266	59.966	11.056		163.01	S
ATOM	6331	CE	MET D	128	−25.311	61.419	10.970		161.60	C
ATOM	6332	H	MET D	128	−20.314	60.209	8.950		129.96	H
ATOM	6333	HA	MET D	128	−22.120	61.539	7.643		131.47	H
ATOM	6334	HB2	MET D	128	−21.701	61.237	10.401		133.41	H
ATOM	6335	HB3	MET D	128	−22.869	62.171	9.871		133.41	H
ATOM	6336	HG2	MET D	128	−23.839	60.301	8.823		150.90	H
ATOM	6337	HG3	MET D	128	−22.710	59.388	9.467		150.90	H
ATOM	6338	HE1	MET D	128	−25.919	61.416	11.726		173.92	H
ATOM	6339	HE2	MET D	128	−24.752	62.212	10.998		173.92	H
ATOM	6340	HE3	MET D	128	−25.814	61.398	10.141		173.92	H
ATOM	6341	N	SER D	129	−19.934	63.362	9.092		127.28	N
ATOM	6342	CA	SER D	129	−19.385	64.711	9.196		130.17	C
ATOM	6343	C	SER D	129	−18.834	65.196	7.859		128.90	C
ATOM	6344	O	SER D	129	−18.574	66.386	7.686		128.22	O
ATOM	6345	CB	SER D	129	−18.286	64.764	10.259		135.60	C
ATOM	6346	OG	SER D	129	−17.121	64.078	9.831		130.81	O
ATOM	6347	H	SER D	129	−19.482	62.766	9.517		132.74	H
ATOM	6348	HA	SER D	129	−20.092	65.318	9.466		136.20	H
ATOM	6349	HB2	SER D	129	−18.059	65.691	10.431		142.72	H
ATOM	6350	HB3	SER D	129	−18.614	64.348	11.072		142.72	H
ATOM	6351	HG	SER D	129	−17.301	63.272	9.680		136.97	H
ATOM	6352	N	GLN D	130	−18.659	64.270	6.920		127.90	N
ATOM	6353	CA	GLN D	130	−18.164	64.603	5.589		125.08	C
ATOM	6354	C	GLN D	130	−19.291	64.546	4.564		125.68	C
ATOM	6355	O	GLN D	130	−19.051	64.318	3.379		125.29	O
ATOM	6356	CB	GLN D	130	−17.035	63.654	5.189		127.46	C
ATOM	6357	CG	GLN D	130	−15.877	63.654	6.167		129.13	C
ATOM	6358	CD	GLN D	130	−14.797	62.669	5.790		126.28	C
ATOM	6359	OE1	GLN D	130	−14.110	62.843	4.786		125.42	O
ATOM	6360	NE2	GLN D	130	−14.637	61.625	6.598		126.08	N
ATOM	6361	H	GLN D	130	−18.821	63.433	7.032		133.48	H
ATOM	6362	HA	GLN D	130	−17.811	65.506	5.599		130.10	H
ATOM	6363	HB2	GLN D	130	−17.385	62.751	5.141		132.95	H
ATOM	6364	HB3	GLN D	130	−16.692	63.922	4.322		132.95	H
ATOM	6365	HG2	GLN D	130	−15.482	64.539	6.190		134.95	H
ATOM	6366	HG3	GLN D	130	−16.207	63.415	7.047		134.95	H
ATOM	6367	HE21	GLN D	130	−14.034	61.036	6.425		131.30	H
ATOM	6368	HE22	GLN D	130	−15.136	61.539	7.293		131.30	H
ATOM	6369	N	ASN D	131	−20.515	64.766	5.035		126.26	N
ATOM	6370	CA	ASN D	131	−21.699	64.750	4.182		129.68	C
ATOM	6371	C	ASN D	131	−21.772	63.462	3.370		128.66	C
ATOM	6372	O	ASN D	131	−21.989	63.485	2.157		126.21	O
ATOM	6373	CB	ASN D	131	−21.704	65.965	3.251		133.82	C
ATOM	6374	CG	ASN D	131	−23.039	66.164	2.559		143.32	C
ATOM	6375	OD1	ASN D	131	−24.084	65.767	3.074		157.86	O
ATOM	6376	ND2	ASN D	131	−23.009	66.779	1.382		151.68	N
ATOM	6377	H	ASN D	131	−20.689	64.929	5.861		131.51	H
ATOM	6378	HA	ASN D	131	−22.490	64.797	4.740		135.61	H
ATOM	6379	HB2	ASN D	131	−21.512	66.761	3.770		140.59	H
ATOM	6380	HB3	ASN D	131	−21.026	65.842	2.568		140.59	H
ATOM	6381	HD21	ASN D	131	−23.740	66.916	0.950		162.02	H
ATOM	6382	HD22	ASN D	131	−22.259	67.041	1.052		162.02	H
ATOM	6383	N	ALA D	132	−21.587	62.341	4.058		129.65	N
ATOM	6384	CA	ALA D	132	−21.549	61.035	3.420		121.47	C
ATOM	6385	C	ALA D	132	−22.010	59.962	4.394		121.23	C
ATOM	6386	O	ALA D	132	−22.408	60.258	5.521		120.92	O
ATOM	6387	CB	ALA D	132	−20.139	60.734	2.924		125.52	C
ATOM	6388	H	ALA D	132	−21.479	62.313	4.911		135.58	H
ATOM	6389	HA	ALA D	132	−22.148	61.033	2.657		125.77	H
ATOM	6390	HB1	ALA D	132	−20.133	59.860	2.502		130.63	H
ATOM	6391	HB2	ALA D	132	−19.879	61.413	2.282		130.63	H
ATOM	6392	HB3	ALA D	132	−19.530	60.741	3.679		130.63	H
ATOM	6393	N	SER D	133	−21.960	58.712	3.950		120.34	N
ATOM	6394	CA	SER D	133	−22.241	57.581	4.818		123.44	C
ATOM	6395	C	SER D	133	−21.204	56.498	4.567		119.78	C
ATOM	6396	O	SER D	133	−20.410	56.591	3.631		121.50	C
ATOM	6397	CB	SER D	133	−23.655	57.042	4.580		125.25	C
ATOM	6398	OG	SER D	133	−23.728	56.304	3.372		129.15	O
ATOM	6399	H	SER D	133	−21.763	58.493	3.142		124.41	H
ATOM	6400	HA	SER D	133	−22.172	57.861	5.744		128.13	H
ATOM	6401	HB2	SER D	133	−23.898	56.461	5.318		130.30	H
ATOM	6402	HB3	SER D	133	−24.272	57.788	4.530		130.30	H
ATOM	6403	HG	SER D	133	−23.521	56.795	2.723		134.98	H
ATOM	6404	N	LEU D	134	−21.197	55.478	5.414		120.00	N
ATOM	6405	CA	LEU D	134	−20.356	54.318	5.176		120.07	C
ATOM	6406	C	LEU D	134	−20.763	53.669	3.859		117.40	C
ATOM	6407	O	LEU D	134	−21.874	53.883	3.376		116.70	O
ATOM	6408	CB	LEU D	134	−20.465	53.326	6.331		120.33	C
ATOM	6409	CG	LEU D	134	−19.715	53.750	7.595		121.63	C
ATOM	6410	CD1	LEU D	134	−20.135	52.914	8.797		122.51	C
ATOM	6411	CD2	LEU D	134	−18.214	53.647	7.381		118.39	C
ATOM	6412	H	LEU D	134	−21.669	55.435	6.132		123.99	H
ATOM	6413	HA	LEU D	134	−19.431	54.601	5.104		124.08	H
ATOM	6414	HB2	LEU D	134	−21.401	53.222	6.565		124.39	H
ATOM	6415	HB3	LEU D	134	−20.102	52.473	6.045		124.39	H
ATOM	6416	HG	LEU D	134	−19.925	54.677	7.789		125.96	H
ATOM	6417	HD11	LEU D	134	−19.640	53.211	9.576		127.02	H
ATOM	6418	HD12	LEU D	134	−21.087	53.030	8.944		127.02	H
ATOM	6419	HD13	LEU D	134	−19.939	51.981	8.616		127.02	H
ATOM	6420	HD21	LEU D	134	−17.760	53.920	8.194		122.07	H
ATOM	6421	HD22	LEU D	134	−17.988	52.728	7.169		122.07	H
ATOM	6422	HD23	LEU D	134	−17.959	54.228	6.648		122.07	H
ATOM	6423	N	LEU D	135	−19.852	52.894	3.279		116.34	N
ATOM	6424	CA	LEU D	135	−20.103	52.208	2.015		115.50	C
ATOM	6425	C	LEU D	135	−21.457	51.505	1.999		113.53	C
ATOM	6426	O	LEU D	135	−21.796	50.755	2.914		117.46	O
ATOM	6427	CB	LEU D	135	−18.996	51.190	1.734		118.55	C
ATOM	6428	CG	LEU D	135	−19.162	50.301	0.498		120.09	C
ATOM	6429	CD1	LEU D	135	−19.189	51.135	−0.777		117.39	C
ATOM	6430	CD2	LEU D	135	−18.048	49.257	0.440		119.20	C
ATOM	6431	H	LEU D	135	−19.068	52.747	3.602		119.60	H
ATOM	6432	HA	LEU D	135	−20.098	52.861	1.298		118.60	H
ATOM	6433	HB2	LEU D	135	−18.163	51.674	1.627		122.27	H
ATOM	6434	HB3	LEU D	135	−18.927	50.601	2.501		122.27	H
ATOM	6435	HG	LEU D	135	−20.007	49.829	0.562		124.11	H
ATOM	6436	HD11	LEU D	135	−19.295	50.543	−1.539		120.87	H
ATOM	6437	HD12	LEU D	135	−19.935	51.754	−0.733		120.87	H
ATOM	6438	HD13	LEU D	135	−18.356	51.625	−0.852		120.87	H
ATOM	6439	HD21	LEU D	135	−18.172	48.707	−0.349		123.04	H
ATOM	6440	HD22	LEU D	135	−17.192	49.712	0.395		123.04	H
ATOM	6441	HD23	LEU D	135	−18.089	48.707	1.238		123.04	H
ATOM	6442	N	LYS D	136	−22.225	51.785	0.953		117.78	N
ATOM	6443	CA	LYS D	136	−23.470	51.084	0.685		121.52	C
ATOM	6444	C	LYS D	136	−23.326	50.350	−0.635		116.54	C
ATOM	6445	O	LYS D	136	−23.061	50.967	−1.664		116.88	O
ATOM	6446	CB	LYS D	136	−24.652	52.054	0.638		121.22	C
ATOM	6447	CG	LYS D	136	−25.972	51.387	0.267		124.56	C
ATOM	6448	CD	LYS D	136	−27.137	52.358	0.370		128.19	C
ATOM	6449	CE	LYS D	136	−28.427	51.738	−0.151		128.08	C
ATOM	6450	NZ	LYS D	136	−29.569	52.692	−0.091		128.58	N1+
ATOM	6451	H	LYS D	136	−22.040	52.391	0.372		121.34	H
ATOM	6452	HA	LYS D	136	−23.633	50.432	1.385		125.82	H
ATOM	6453	HB2	LYS D	136	−24.759	52.460	1.512		125.47	H
ATOM	6454	HB3	LYS D	136	−24.468	52.739	−0.024		125.47	H
ATOM	6455	HG2	LYS D	136	−25.923	51.067	−0.648		129.47	H
ATOM	6456	HG3	LYS D	136	−26.138	50.648	0.872		129.47	H
ATOM	6457	HD2	LYS D	136	−27.270	52.601	1.300		133.82	H
ATOM	6458	HD3	LYS D	136	−26.944	53.148	−0.159		133.82	H
ATOM	6459	HE2	LYS D	136	−28.302	51.473	−1.076		133.70	H
ATOM	6460	HE3	LYS D		136	−28.650	50.965	0.391		133.70	H
ATOM	6461	HZ1	LYS D	136	−30.307	52.302	−0.401		134.29	H
ATOM	6462	HZ2	LYS D	136	−29.708	52.947	0.751		134.29	H
ATOM	6463	HZ3	LYS D	136	−29.391	53.410	−0.585		134.29	H
ATOM	6464	N	VAL D		137	−23.490	49.032	−0.592		115.00	N
ATOM	6465	CA	VAL D	137	−23.377	48.194	−1.777		114.80	C
ATOM	6466	C	VAL D		137	−24.767	47.914	−2.328		115.82	C
ATOM	6467	O	VAL D		137	−25.542	47.181	−1.714		117.01	O
ATOM	6468	CB	VAL D	137	−22.661	46.870	−1.462		118.73	C
ATOM	6469	CG1	VAL D	137	−22.505	46.037	−2.723		121.27	C
ATOM	6470	CG2	VAL D	137	−21.293	47.142	−0.828		119.01	C
ATOM	6471	H	VAL D		137	−23.670	48.594	0.126		118.00	H
ATOM	6472	HA	VAL D	137	−22.867	48.663	−2.456		117.76	H
ATOM	6473	HB	VAL D	137	−23.193	46.363	−0.829		122.47	H
ATOM	6474	HG11	VAL D	137	−22.052	45.209	−2.500		125.53	H
ATOM	6475	HG12	VAL D	137	−23.384	45.846	−3.086		125.53	H
ATOM	6476	HG13	VAL D	137	−21.981	46.537	−3.368		125.53	H
ATOM	6477	HG21	VAL D	137	−20.859	46.296	−0.638		122.82	H
ATOM	6478	HG22	VAL D	137	−20.755	47.658	−1.449		122.82	H
ATOM	6479	HG23	VAL D	137	−21.420	47.641	−0.006		122.82	H
ATOM	6480	N	TYR D	138	−25.068	48.500	−3.485		115.98	N
ATOM	6481	CA	TYR D	138	−26.410	48.453	−4.061		120.40	C
ATOM	6482	C	TYR D	138	−26.439	47.849	−5.467		119.25	C
ATOM	6483	O	TYR D	138	−27.512	47.551	−5.991		119.44	O
ATOM	6484	CB	TYR D	138	−27.006	49.865	−4.106		116.40	C
ATOM	6485	CG	TYR D	138	−26.405	50.758	−5.170		115.53	C
ATOM	6486	CD1	TYR D	138	−26.952	50.820	−6.446		118.12	C
ATOM	6487	CD2	TYR D	138	−25.293	51.544	−4.897		120.57	C
ATOM	6488	CE1	TYR D	138	−26.406	51.635	−7.419		118.07	C
ATOM	6489	CE2	TYR D	138	−24.742	52.366	−5.864		114.74	C
ATOM	6490	CZ	TYR D	138	−25.298	52.407	−7.121		119.68	C
ATOM	6491	OH	TYR D	138	−24.748	53.225	−8.080		118.98	O
ATOM	6492	H	TYR D	138	−24.502	48.937	−3.963		119.18	H
ATOM	6493	HA	TYR D	138	−26.976	47.909	−3.492		124.48	H
ATOM	6494	HB2	TYR D	138	−27.958	49.795	−4.283		119.68	H
ATOM	6495	HB3	TYR D	138	−26.863	50.291	−3.247		119.68	H
ATOM	6496	HD1	TYR D	138	−27.696	50.301	−6.650		121.75	H
ATOM	6497	HD2	TYR D	138	−24.913	51.519	−4.049		124.68	H
ATOM	6498	HE1	TYR D	138	−26.782	51.666	−8.269		121.68	H
ATOM	6499	HE2	TYR D	138	−23.996	52.885	−5.666		117.69	H
ATOM	6500	HH	TYR D	138	−25.181	53.160	−8.797		122.78	H
ATOM	6501	N	SER D	139	−25.271	47.667	−6.080		118.67	N
ATOM	6502	CA	SER D	139	−25.222	47.169	−7.456		120.25	C
ATOM	6503	C	SER D	139	−23.873	46.574	−7.844		124.81	C
ATOM	6504	O	SER D	139	−22.843	47.241	−7.753		116.53	O
ATOM	6505	CB	SER D	139	−25.563	48.296	−8.428		118.66	C
ATOM	6506	OG	SER D	139	−25.305	47.903	−9.763		122.13	O
ATOM	6507	H	SER D	139	−24.502	47.821	−5.728		122.40	H
ATOM	6508	HA	SER D	139	−25.891	46.475	−7.560		124.30	H
ATOM	6509	HB2	SER D	139	−26.504	48.515	−8.339		122.39	H
ATOM	6510	HB3	SER D	139	−25.021	49.071	−8.216		122.39	H
ATOM	6511	HG	SER D	139	−25.496	48.530	−10.289		126.55	H
ATOM	6512	N	LYS D	140	−23.891	45.327	−8.307		122.07	N
ATOM	6513	CA	LYS D	140	−22.670	44.654	−8.737		122.87	C
ATOM	6514	C	LYS D	140	−22.131	45.225	−10.041		125.49	C
ATOM	6515	O	LYS D	140	−20.981	44.981	−10.396		128.27	O
ATOM	6516	CB	LYS D	140	−22.907	43.153	−8.904		125.37	C
ATOM	6517	CG	LYS D	140	−22.861	42.373	−7.607		128.96	C
ATOM	6518	CD	LYS D	140	−22.757	40.877	−7.865		134.51	C
ATOM	6519	CE	LYS D	140	−22.573	40.100	−6.570		136.49	C
ATOM	6520	NZ	LYS D	140	−22.353	38.648	−6.819		149.97	N1+
ATOM	6521	H	LYS D		140	−24.601	44.848	−8.383		126.49	H
ATOM	6522	HA	LYS D		140	−21.990	44.774	−8.056		127.44	H
ATOM	6523	HB2	LYS D	140	−23.783	43.018	−9.299		130.45	H
ATOM	6524	HB3	LYS D	140	−22.224	42.792	−9.491		130.45	H
ATOM	6525	HG2	LYS D	140	−22.085	42.648	−7.094		134.76	H
ATOM	6526	HG3	LYS D		140	−23.673	42.539	−7.103		134.76	H
ATOM	6527	HD2	LYS D		140	−23.571	40.568	−8.292		141.41	H
ATOM	6528	HD3	LYS D	140	−21.992	40.703	−8.435		141.41	H
ATOM	6529	HE2	LYS D	140	−21.801	40.447	−6.097		143.79	H
ATOM	6530	HE3	LYS D		140	−23.370	40.196	−6.025		143.79	H
ATOM	6531	HZ1	LYS D	140	−22.249	38.220	−6.046		159.97	H
ATOM	6532	HZ2	LYS D	140	−23.051	38.304	−7.249		159.97	H
ATOM	6533	HZ3	LYS D	140	−21.622	38.532	−7.314		159.97	H
ATOM	6534	N	GLU D	141	−22.959	45.974	−10.758		121.06	N
ATOM	6535	CA	GLU D	141	−22.523	46.596	−12.001		123.91	C
ATOM	6536	C	GLU D	141	−21.994	48.009	−11.753		124.83	C
ATOM	6537	O	GLU D	141	−20.867	48.325	−12.135		123.48	O
ATOM	6538	CB	GLU D	141	−23.666	46.614	−13.015		131.80	C
ATOM	6539	CG	GLU D	141	−23.913	45.254	−13.656		135.80	C
ATOM	6540	CD	GLU D	141	−25.007	45.285	−14.707		140.22	C
ATOM	6541	OE1	GLU D	141	−26.098	45.818	−14.415		142.25	O
ATOM	6542	OE2	GLU D	141	−24.775	44.777	−15.825		136.77	O1−
ATOM	6543	H	GLU D	141	−23.776	46.138	−10.547		125.27	H
ATOM	6544	HA	GLU D	141	−21.800	46.070	−12.378		128.69	H
ATOM	6545	HB2	GLU D	141	−24.482	46.886	−12.566		138.16	H
ATOM	6546	HB3	GLU D	141	−23.451	47.243	−13.722		138.16	H
ATOM	6547	HG2	GLU D	141	−23.096	44.954	−14.084		142.96	H
ATOM	6548	HG3	GLU D	141	−24.178	44.624	−12.968		142.96	H
ATOM	6549	N	ASP D	142	−22.795	48.851	−11.106		122.91	N
ATOM	6550	CA	ASP D	142	−22.382	50.226	−10.809		121.81	C
ATOM	6551	C	ASP D	142	−21.179	50.272	−9.870		117.14	C
ATOM	6552	O	ASP D	142	−20.484	51.284	−9.793		118.60	O
ATOM	6553	CB	ASP D	142	−23.534	51.015	−10.182		123.08	C
ATOM	6554	CG	ASP D	142	−24.591	51.429	−11.192		129.65	C
ATOM	6555	OD1	ASP D	142	−24.549	50.952	−12.347		132.81	O
ATOM	6556	OD2	ASP D	142	−25.474	52.232	−10.819		129.12	O1−
ATOM	6557	H	ASP D	142	−23.584	48.654	−10.827		127.49	H
ATOM	6558	HA	ASP D	142	−22.133	50.666	−11.637		126.17	H
ATOM	6559	HB2	ASP D	142	−23.963	50.465	−9.508		127.70	H
ATOM	6560	HB3	ASP D	142	−23.179	51.821	−9.774		127.70	H
ATOM	6561	N	GLN D	143	−20.951	49.180	−9.149		117.82	N
ATOM	6562	CA	GLN D	143	−19.869	49.108	−8.173		120.33	C
ATOM	6563	C	GLN D	143	−19.029	47.858	−8.395		117.41	C
ATOM	6564	O	GLN D	143	−18.528	47.255	−7.444		116.39	O
ATOM	6565	CB	GLN D	143	−20.433	49.119	−6.754		116.84	C
ATOM	6566	CG	GLN D	143	−21.350	50.301	−6.464		119.15	C
ATOM	6567	CD	GLN D	143	−21.996	50.201	−5.100		115.77	C
ATOM	6568	OE1	GLN D	143	−22.746	49.264	−4.827		118.59	O
ATOM	6569	NE2	GLN D	143	−21.696	51.156	−4.229		114.45	N
ATOM	6570	H	GLN D	143	−21.414	48.458	−9.208		121.39	H
ATOM	6571	HA	GLN D	143	−19.294	49.882	−8.276		124.40	H
ATOM	6572	HB2	GLN D	143	−20.944	48.306	−6.615		120.21	H
ATOM	6573	HB3	GLN D	143	−19.695	49.155	−6.125		120.21	H
ATOM	6574	HG2	GLN D	143	−20.832	51.120	−6.493		122.98	H
ATOM	6575	HG3	GLN D	143	−22.054	50.327	−7.130		122.98	H
ATOM	6576	HE21	GLN D	143	−22.039	51.141	−3.440		117.34	H
ATOM	6577	HE22	GLN D	143	−21.159	51.789	−4.453		117.34	H
ATOM	6578	N	ASP D	144	−18.880	47.478	−9.659		118.01	N
ATOM	6579	CA	ASP D	144	−18.187	46.248	−10.016		119.97	C
ATOM	6580	C	ASP D	144	−16.735	46.242	−9.540		119.34	C
ATOM	6581	O	ASP D	144	−16.177	45.186	−9.256		120.61	O
ATOM	6582	CB	ASP D	144	−18.247	46.025	−11.534		122.96	C
ATOM	6583	CG	ASP D	144	−17.787	47.234	−12.330		126.02	C
ATOM	6584	OD1	ASP D	144	−17.622	48.322	−11.741		122.89	O
ATOM	6585	OD2	ASP D	144	−17.611	47.097	−13.558		129.55	O1−
ATOM	6586	H	ASP D	144	−19.175	47.921	−10.335		121.62	H
ATOM	6587	HA	ASP D	144	−18.639	45.503	−9.590		123.97	H
ATOM	6588	HB2	ASP D	144	−17.672	45.278	−11.765		127.56	H
ATOM	6589	HB3	ASP D	144	−19.162	45.830	−11.788		127.56	H
ATOM	6590	N	LEU D	145	−16.128	47.417	−9.434		117.08	N
ATOM	6591	CA	LEU D	145	−14.718	47.487	−9.074		121.64	C
ATOM	6592	C	LEU D	145	−14.485	47.240	−7.581		119.33	C
ATOM	6593	O	LEU D	145	−13.340	47.192	−7.132		118.18	O
ATOM	6594	CB	LEU D	145	−14.139	48.835	−9.498		122.74	C
ATOM	6595	CG	LEU D	145	−14.106	49.032	−11.021		127.25	C
ATOM	6596	CD1	LEU D	145	−13.556	50.397	−11.374		129.85	C
ATOM	6597	CD2	LEU D	145	−13.283	47.949	−11.725		130.04	C
ATOM	6598	H	LEU D	145	−16.504	48.179	−9.563		120.50	H
ATOM	6599	HA	LEU D	145	−14.240	46.798	−9.562		125.97	H
ATOM	6600	HB2	LEU D	145	−14.683	49.543	−9.118		127.29	H
ATOM	6601	HB3	LEU D	145	−13.230	48.905	−9.168		127.29	H
ATOM	6602	HG	LEU D	145	−15.013	48.982	−11.361		132.69	H
ATOM	6603	HD11	LEU D	145	−13.546	50.493	−12.339		135.82	H
ATOM	6604	HD12	LEU D	145	−14.123	51.077	−10.979		135.82	H
ATOM	6605	HD13	LEU D	145	−12.654	50.474	−11.024		135.82	H
ATOM	6606	HD21	LEU D	145	−13.293	48.117	−12.680		136.04	H
ATOM	6607	HD22	LEU D	145	−12.372	47.979	−11.392		136.04	H
ATOM	6608	HD23	LEU D	145	−13.676	47.082	−11.537		136.04	H
ATOM	6609	N	LEU D	146	−15.561	47.059	−6.818		114.34	N
ATOM	6610	CA	LEU D	146	−15.431	46.629	−5.427		115.08	C
ATOM	6611	C	LEU D	146	−14.819	45.229	−5.369		115.01	C
ATOM	6612	O	LEU D	146	−14.308	44.808	−4.332		116.15	O
ATOM	6613	CB	LEU D	146	−16.784	46.644	−4.710		119.54	C
ATOM	6614	CG	LEU D	146	−17.430	48.005	−4.436		117.93	C
ATOM	6615	CD1	LEU D	146	−18.798	47.820	−3.797		117.26	C
ATOM	6616	CD2	LEU D	146	−16.545	48.849	−3.537		118.06	C
ATOM	6617	H	LEU D	146	−16.372	47.177	−7.079		117.21	H
ATOM	6618	HA	LEU D	146	−14.836	47.238	−4.961		118.10	H
ATOM	6619	HB2	LEU D	146	−17.413	46.135	−5.246		123.45	H
ATOM	6620	HB3	LEU D	146	−16.673	46.206	−3.851		123.45	H
ATOM	6621	HG	LEU D	146	−17.548	48.477	−5.275		121.51	H
ATOM	6622	HD11	LEU D	146	−19.189	48.692	−3.632		120.71	H
ATOM	6623	HD12	LEU D	146	−19.362	47.312	−4.400		120.71	H
ATOM	6624	HD13	LEU D	146	−18.692	47.340	−2.960		120.71	H
ATOM	6625	HD21	LEU D	146	−16.977	49.703	−3.381		121.67	H
ATOM	6626	HD22	LEU D	146	−16.416	48.384	−2.695		121.67	H
ATOM	6627	HD23	LEU D	146	−15.689	48.986	−3.974		121.67	H
ATOM	6628	N	LYS D	147	−14.872	44.513	−6.490		114.65	N
ATOM	6629	CA	LYS D	147	−14.213	43.214	−6.620		117.93	C
ATOM	6630	C	LYS D	147	−12.713	43.325	−6.339		115.43	C
ATOM	6631	O	LYS D	147	−12.098	42.393	−5.821		116.29	O
ATOM	6632	CB	LYS D	147	−14.423	42.649	−8.031		122.58	C
ATOM	6633	CG	LYS D	147	−13.517	43.312	−9.070		145.24	C
ATOM	6634	CD	LYS D	147	−13.950	43.075	−10.516		179.42	C
ATOM	6635	CE	LYS D	147	−13.696	44.304	−11.398		190.15	C
ATOM	6636	NZ	LYS D	147	−12.667	44.084	−12.457		103.814	N1+
ATOM	6637	H	LYS D	147	−15.290	44.761	−7.199		117.58	H
ATOM	6638	HA	LYS D	147	−14.598	42.593	−5.982		121.51	H
ATOM	6639	HB2	LYS D	147	−14.228	41.699	−8.024		127.09	H
ATOM	6640	HB3	LYS D	147	−15.344	42.796	−8.298		127.09	H
ATOM	6641	HG2	LYS D	147	−13.514	44.269	−8.915		154.29	H
ATOM	6642	HG3	LYS D	147	−12.618	42.961	−8.969		154.29	H
ATOM	6643	HD2	LYS D	147	−13.447	42.331	−10.882		195.30	H
ATOM	6644	HD3	LYS D	147	−14.900	42.879	−10.536		195.30	H
ATOM	6645	HE2	LYS D	147	−14.526	44.550	−11.837		108.118	H
ATOM	6646	HE3	LYS D	147	−13.392	45.034	−10.836		108.118	H
ATOM	6647	HZ1	LYS D	147	−12.923	43.424	−12.998		124.611	H
ATOM	6648	HZ2	LYS D	147	−12.561	44.826	−12.937		124.611	H
ATOM	6649	HZ3	LYS D	147	−11.889	43.866	−12.085		124.6	H
ATOM	6650	N	LEU D	148	−12.136	44.472	−6.685		114.11	N
ATOM	6651	CA	LEU D	148	−10.686	44.663	−6.635		114.27	C
ATOM	6652	C	LEU D		148	−10.199	45.320	−5.346		114.62	C
ATOM	6653	O	LEU D	148	−9.001	45.581	−5.189		117.22	O
ATOM	6654	CB	LEU D	148	−10.235	45.508	−7.827		114.41	C
ATOM	6655	CG	LEU D	148	−10.319	44.864	−9.212		121.00	C
ATOM	6656	CD1	LEU D	148	−9.959	45.879	−10.272		122.02	C
ATOM	6657	CD2	LEU D		148	−9.408	43.651	−9.311		124.34	C
ATOM	6658	H	LEU D		148	−12.567	45.165	−6.956		116.94	H
ATOM	6659	HA	LEU D	148	−10.256	43.797	−6.706		117.12	H
ATOM	6660	HB2	LEU D	148	−10.780	46.309	−7.852		117.29	H
ATOM	6661	HB3	LEU D	148	−9.308	45.758	−7.685		117.29	H
ATOM	6662	HG	LEU D		148	−11.230	44.571	−9.371		125.20	H
ATOM	6663	HD11	LEU D	148	−10.016	45.457	−11.144		126.42	H
ATOM	6664	HD12	LEU D	148	−10.580	46.622	−10.222		126.42	H
ATOM	6665	HD13	LEU D	148	−9.054	46.192	−10.115		126.42	H
ATOM	6666	HD21	LEU D	148	−9.487	43.270	−10.199		129.20	H
ATOM	6667	HD22	LEU D	148	−8.493	43.930	−9.151		129.20	H
ATOM	6668	HD23	LEU D	148	−9.677	42.999	−8.645		129.20	H
ATOM	6669	N	VAL D		149	−11.114	45.590	−4.424		118.94	N
ATOM	6670	CA	VAL D	149	−10.744	46.245	−3.176		118.09	C
ATOM	6671	O	VAL D	149	−9.970	45.299	−2.268		114.58	C
ATOM	6672	O	VAL D		149	−10.466	44.240	−1.876		114.09	O
ATOM	6673	CB	VAL D	149	−11.983	46.778	−2.430		119.00	C
ATOM	6674	CG1	VAL D	149	−11.624	47.240	−1.013		115.72	C
ATOM	6675	CG2	VAL D	149	−12.601	47.914	−3.214		115.52	C
ATOM	6676	H	VAL D		149	−11.951	45.406	−4.495		122.73	H
ATOM	6677	HA	VAL D	149	−10.170	47.001	−3.377		121.71	H
ATOM	6678	HB	VAL D	149	−12.640	46.068	−2.359		122.80	H
ATOM	6679	HG11	VAL D	149	−12.426	47.568	−0.576		118.87	H
ATOM	6680	HG12	VAL D	149	−11.261	46.489	−0.519		118.87	H
ATOM	6681	HG13	VAL D	149	−10.964	47.949	−1.070		118.87	H
ATOM	6682	HG21	VAL D	149	−13.379	48.240	−2.736		118.62	H
ATOM	6683	HG22	VAL D	149	−11.947	48.624	−3.309		118.62	H
ATOM	6684	HG23	VAL D	149	−12.863	47.587	−4.089		118.62	H
ATOM	6685	N	LYS D	150	−8.748	45.704	−1.934		111.38	N
ATOM	6686	CA	LYS D	150	−7.897	44.949	−1.021		113.03	C
ATOM	6687	C	LYS D	150	−8.243	45.267	0.428		112.12	C
ATOM	6688	O	LYS D	150	−8.703	46.366	0.733		111.51	O
ATOM	6689	CB	LYS D	150	−6.421	45.270	−1.290		115.75	C
ATOM	6690	CG	LYS D	150	−5.427	44.415	−0.510		118.85	C
ATOM	6691	CD	LYS D	150	−4.028	45.031	−0.525		125.97	C
ATOM	6692	CE	LYS D	150	−2.999	44.123	−1.170		128.15	C
ATOM	6693	NZ	LYS D	150	−2.862	42.800	−0.512		127.44	N1+
ATOM	6694	H	LYS D		150	−8.384	46.425	−2.228		113.65	H
ATOM	6695	HA	LYS D	150	−8.034	43.999	−1.166		115.63	H
ATOM	6696	HB2	LYS D	150	−6.243	45.139	−2.234		118.90	H
ATOM	6697	HB3	LYS D	150	−6.259	46.197	−1.054		118.90	H
ATOM	6698	HG2	LYS D	150	−5.719	44.345	0.412		122.62	H
ATOM	6699	HG3	LYS D	150	−5.376	43.535	−0.914		122.62	H
ATOM	6700	HD2	LYS D	150	−4.053	45.861	−1.027		131.17	H
ATOM	6701	HD3	LYS D	150	−3.748	45.203	0.388		131.17	H
ATOM	6702	HE2	LYS D	150	−3.254	43.968	−2.093		133.78	H
ATOM	6703	HE3	LYS D	150	−2.133	44.560	−1.137		133.78	H
ATOM	6704	HZ1	LYS D	150	−3.639	42.367	−0.535		132.92	H
ATOM	6705	HZ2	LYS D	150	−2.246	42.314	−0.932		132.92	H
ATOM	6706	HZ3	LYS D	150	−2.616	42.907	0.337		132.92	H
ATOM	6707	N	SER D	151	−8.011	44.299	1.308		19.93	N
ATOM	6708	CA	SER D	151	−8.161	44.483	2.751		117.48	C
ATOM	6709	C	SER D	151	−9.629	44.513	3.165		115.32	C
ATOM	6710	O	SER D	151	−10.520	44.226	2.361		111.83	O
ATOM	6711	CB	SER D	151	−7.461	45.765	3.220		114.44	C
ATOM	6712	OG	SER D	151	−7.316	45.776	4.629		115.79	O
ATOM	6713	H	SER D	151	−7.760	43.506	1.090		111.92	H
ATOM	6714	HA	SER D	151	−7.742	43.735	3.205		120.98	H
ATOM	6715	HB2	SER D	151	−6.582	45.812	2.812		117.33	H
ATOM	6716	HB3	SER D	151	−7.993	46.531	2.952		117.33	H
ATOM	6717	HG	SER D	151	−6.857	45.117	4.875		118.95	H
ATOM	6718	N	TYR D	152	−9.849	44.872	4.428		114.15	N
ATOM	6719	CA	TYR D	152	−11.134	44.731	5.099		114.23	C
ATOM	6720	0	TYR D	152	−11.546	46.065	5.719		115.88	C
ATOM	6721	O	TYR D	152	−10.765	46.681	6.436		115.07	O
ATOM	6722	CB	TYR D	152	−11.037	43.620	6.152		114.66	C
ATOM	6723	CG	TYR D	152	−10.793	42.275	5.507		114.16	C
ATOM	6724	CD1	TYR D	152	−9.544	41.942	4.993		116.37	C
ATOM	6725	CD2	TYR D	152	−11.819	41.354	5.375		112.96	C
ATOM	6726	CE1	TYR D	152	−9.327	40.728	4.372		116.79	C
ATOM	6727	CE2	TYR D	152	−11.611	40.138	4.758		117.09	C
ATOM	6728	CZ	TYR D	152	−10.365	39.830	4.257		115.39	C
ATOM	6729	OH	TYR D	152	−10.164	38.616	3.641		119.34	O
ATOM	6730	H	TYR D	152	−9.243	45.214	4.934		116.98	H
ATOM	6731	HA	TYR D	152	−11.809	44.477	4.449		117.08	H
ATOM	6732	HB2	TYR D	152	−10.298	43.809	6.751		117.59	H
ATOM	6733	HB3	TYR D	152	−11.870	43.574	6.647		117.59	H
ATOM	6734	HD1	TYR D	152	−8.845	42.551	5.062		119.64	H
ATOM	6735	HD2	TYR D	152	−12.664	41.561	5.704		115.55	H
ATOM	6736	HE1	TYR D	152	−8.486	40.518	4.035		120.15	H
ATOM	6737	HE2	TYR D	152	−12.309	39.529	4.679		120.50	H
ATOM	6738	HH	TYR D	152	−10.877	38.172	3.641		123.21	H
ATOM	6739	N	HIS D	153	−12.762	46.519	5.418		115.60	N
ATOM	6740	CA	HIS D	153	−13.195	47.868	5.791		114.87	C
ATOM	6741	C	HIS D	153	−14.638	47.906	6.274		115.50	C
ATOM	6742	O	HIS D	153	−15.492	47.185	5.761		115.53	O
ATOM	6743	CB	HIS D	153	−13.048	48.819	4.603		114.96	C
ATOM	6744	CG	HIS D	153	−11.822	48.574	3.783		117.33	C
ATOM	6745	ND1	HIS D	153	−10.655	49.285	3.958		114.80	N
ATOM	6746	CD2	HIS D	153	−11.579	47.690	2.786		115.17	C
ATOM	6747	CE1	HIS D	153	−9.747	48.853	3.100		117.80	C
ATOM	6748	NE2	HIS D	153	−10.283	47.885	2.377		114.81	N
ATOM	6749	H	HIS D	153	−13.358	46.064	4.996		118.72	H
ATOM	6750	HA	HIS D	153	−12.630	48.194	6.509		117.84	H
ATOM	6751	HB2	HIS D	153	−13.819	48.715	4.023		117.95	H
ATOM	6752	HB3	HIS D	153	−13.007	49.730	4.935		117.95	H
ATOM	6753	HD1	HIS D	153	−10.537	49.914	4.533		117.76	H
ATOM	6754	HD2	HIS D	153	−12.179	47.069	2.441		118.21	H
ATOM	6755	HE1	HIS D	153	−8.879	49.175	3.020		121.36	H
ATOM	6756	HE2	HIS D	153	−9.884	47.448	1.753		117.77	H
ATOM	6757	N	TRP D	154	−14.911	48.764	7.251		114.83	N
ATOM	6758	CA	TRP D	154	−16.280	48.975	7.703		118.59	C
ATOM	6759	C	TRP D	154	−17.160	49.471	6.558		116.71	C
ATOM	6760	O	TRP D	154	−16.792	50.405	5.843		115.23	O
ATOM	6761	CB	TRP D	154	−16.340	49.994	8.849		120.54	C
ATOM	6762	CG	TRP D	154	−15.871	49.510	10.190		119.81	C
ATOM	6763	CD1	TRP D	154	−14.965	50.126	11.007		123.78	C
ATOM	6764	CD2	TRP D	154	−16.298	48.331	10.886		121.11	C
ATOM	6765	NE1	TRP D	154	−14.798	49.402	12.160		123.26	N
ATOM	6766	CE2	TRP D	154	−15.602	48.295	12.112		123.65	C
ATOM	6767	CE3	TRP D	154	−17.194	47.300	10.591		119.42	C
ATOM	6768	CZ2	TRP D	154	−15.774	47.269	13.040		125.29	C
ATOM	6769	CZ3	TRP D	154	−17.362	46.281	11.514		122.46	C
ATOM	6770	CH2	TRP D	154	−16.657	46.275	12.723		125.53	C
ATOM	6771	H	TRP D	154	−14.324	49.234	7.667		117.80	H
ATOM	6772	HA	TRP D	154	−16.644	48.135	8.024		122.30	H
ATOM	6773	HB2	TRP D	154	−15.789	50.756	8.609		124.65	H
ATOM	6774	HB3	TRP D	154	−17.260	50.283	8.952		124.65	H
ATOM	6775	HD1	TRP D	154	−14.527	50.922	10.811		128.53	H
ATOM	6776	HE1	TRP D	154	−14.270	49.609	12.808		127.92	H
ATOM	6777	HE3	TRP D	154	−17.667	47.298	9.790		123.30	H
ATOM	6778	HZ2	TRP D	154	−15.305	47.261	13.843		130.35	H
ATOM	6779	HZ3	TRP D	154	−17.957	45.591	11.329		126.95	H
ATOM	6780	HH2	TRP D	154	−16.791	45.577	13.323		130.63	H
ATOM	6781	N	MET D	155	−18.321	48.845	6.392		116.33	N
ATOM	6782	CA	MET D	155	−19.362	49.379	5.519		114.51	C
ATOM	6783	C	MET D	155	−20.595	49.713	6.361		117.12	C
ATOM	6784	O	MET D	155	−20.603	49.497	7.573		119.71	O
ATOM	6785	CB	MET D	155	−19.704	48.392	4.397		115.94	C
ATOM	6786	CG	MET D	155	−19.896	46.957	4.840		116.64	C
ATOM	6787	SD	MET D	155	−20.468	45.915	3.480		119.78	S
ATOM	6788	CE	MET D	155	−20.186	44.291	4.179		121.22	C
ATOM	6789	H	MET D	155	−18.533	48.105	6.776		119.60	H
ATOM	6790	HA	MET D	155	−19.035	50.194	5.107		117.42	H
ATOM	6791	HB2	MET D	155	−20.528	48.680	3.974		119.13	H
ATOM	6792	HB3	MET D	155	−18.984	48.403	3.747		119.13	H
ATOM	6793	HG2	MET D	155	−19.050	46.605	5.158		119.97	H
ATOM	6794	HG3	MET D	155	−20.560	46.927	5.547		119.97	H
ATOM	6795	HE1	MET D	155	−20.458	43.619	3.535		125.46	H
ATOM	6796	HE2	MET D	155	−19.242	44.194	4.381		125.46	H
ATOM	6797	HE3	MET D	155	−20.709	44.202	4.992		125.46	H
ATOM	6798	N	GLY D	156	−21.629	50.248	5.719		119.69	N
ATOM	6799	CA	GLY D	156	−22.778	50.784	6.429		120.08	C
ATOM	6800	C	GLY D	156	−23.884	49.782	6.697		127.40	C
ATOM	6801	O	GLY D	156	−25.047	50.157	6.856		125.15	O
ATOM	6802	H	GLY D	156	−21.686	50.313	4.863		123.63	H
ATOM	6803	HA2	GLY D	156	−22.484	51.139	7.282		124.09	H
ATOM	6804	HA3	GLY D	156	−23.155	51.514	5.913		124.09	H
ATOM	6805	N	LEU D	157	−23.523	48.505	6.755		122.24	N
ATOM	6806	CA	LEU D	157	−24.486	47.457	7.038		124.99	C
ATOM	6807	0	LEU D	157	−24.748	47.391	8.542		132.61	C
ATOM	6808	O	LEU D	157	−23.816	47.402	9.348		132.90	O
ATOM	6809	CB	LEU D	157	−23.981	46.116	6.506		127.86	C
ATOM	6810	CG	LEU D	157	−25.030	45.102	6.053		131.65	C
ATOM	6811	CD1	LEU D	157	−25.857	45.622	4.884		133.53	C
ATOM	6812	CD2	LEU D	157	−24.345	43.799	5.675		134.82	C
ATOM	6813	H	LEU D	157	−22.720	48.221	6.632		126.69	H
ATOM	6814	HA	LEU D	157	−25.323	47.663	6.594		129.98	H
ATOM	6815	HB2	LEU D	157	−23.408	46.293	5.743		133.43	H
ATOM	6816	HB3	LEU D	157	−23.459	45.693	7.205		133.43	H
ATOM	6817	HG	LEU D	157	−25.633	44.921	6.790		137.98	H
ATOM	6818	HD11	LEU D	157	−26.507	44.947	4.632		140.23	H
ATOM	6819	HD12	LEU D	157	−26.312	46.434	5.156		140.23	H
ATOM	6820	HD13	LEU D	157	−25.266	45.808	4.137		140.23	H
ATOM	6821	HD21	LEU D	157	−25.017	43.161	5.389		141.79	H
ATOM	6822	HD22	LEU D	157	−23.720	43.968	4.953		141.79	H
ATOM	6823	HD23	LEU D	157	−23.871	43.456	6.449		141.79	H
ATOM	6824	N	VAL D	158	−26.026	47.342	8.902		133.79	N
ATOM	6825	CA	VAL D	158	−26.462	47.376	10.293		134.56	C
ATOM	6826	C	VAL D	158	−27.282	46.133	10.623		140.45	C
ATOM	6827	O	VAL D	158	−28.183	45.762	9.871		138.74	O
ATOM	6828	CB	VAL D	158	−27.307	48.635	10.579		131.82	C
ATOM	6829	CG1	VAL D	158	−27.896	48.591	11.984		145.90	C
ATOM	6830	CG2	VAL D	158	−26.472	49.890	10.392		135.55	C
ATOM	6831	H	VAL D	158	−26.677	47.288	8.342		140.54	H
ATOM	6832	HA	VAL D	158	−25.685	47.392	10.873		141.47	H
ATOM	6833	HB	VAL D	158	−28.043	48.669	9.948		138.18	H
ATOM	6834	HG11	VAL D	158	−28.419	49.394	12.131		155.08	H
ATOM	6835	HG12	VAL D	158	−28.461	47.807	12.064		155.08	H
ATOM	6836	HG13	VAL D	158	−27.172	48.545	12.628		155.08	H
ATOM	6837	HG21	VAL D	158	−27.024	50.666	10.577		142.66	H
ATOM	6838	HG22	VAL D	158	−25.721	49.863	11.006		142.66	H
ATOM	6839	HG23	VAL D	158	−26.151	49.922	9.477		142.66	H
ATOM	6840	N	HIS D	159	−26.974	45.501	11.751		142.21	N
ATOM	6841	CA	HIS D	159	−27.698	44.309	12.176		147.51	C
ATOM	6842	C	HIS D	159	−28.905	44.685	13.029		156.08	C
ATOM	6843	O	HIS D	159	−28.829	45.584	13.867		151.08	O
ATOM	6844	CB	HIS D	159	−26.785	43.370	12.962		148.52	C
ATOM	6845	CG	HIS D	159	−27.304	41.969	13.065		150.74	C
ATOM	6846	ND1	HIS D	159	−26.815	41.062	13.981		152.54	N
ATOM	6847	CD2	HIS D	159	−28.266	41.318	12.369		156.93	C
ATOM	6848	CE1	HIS D	159	−27.454	39.914	13.845		163.50	C
ATOM	6849	NE2	HIS D	159	−28.340	40.043	12.874		164.61	N
ATOM	6850	H	HIS D	159	−26.348	45.743	12.289		150.65	H
ATOM	6851	HA	HIS D	159	−28.018	43.835	11.392		157.02	H
ATOM	6852	HB2	HIS D	159	−25.920	43.334	12.524		158.23	H
ATOM	6853	HB3	HIS D	159	−26.683	43.715	13.863		158.23	H
ATOM	6854	HD1	HIS D	159	−26.191	41.219	14.552		163.05	H
ATOM	6855	HD2	HIS D	159	−28.781	41.669	11.679		168.31	H
ATOM	6856	HE1	HIS D	159	−27.305	39.145	14.347		176.20	H
ATOM	6857	HE2	HIS D	159	−28.875	39.427	12.601		177.54	H
ATOM	6858	N	ILE D	160	−30.011	43.984	12.807		160.19	N
ATOM	6859	CA	ILE D	160	−31.243	44.209	13.553		172.28	C
ATOM	6860	C	ILE D	160	−31.530	43.001	14.446		184.70	C
ATOM	6861	O	ILE D	160	−31.991	41.970	13.955		184.61	O
ATOM	6862	CB	ILE D	160	−32.433	44.447	12.609		173.35	C
ATOM	6863	CG1	ILE D	160	−32.142	45.623	11.674		159.74	C
ATOM	6864	CG2	ILE D	160	−33.694	44.725	13.407		185.05	C
ATOM	6865	CD1	ILE D	160	−33.047	45.674	10.476		164.40	C
ATOM	6866	H	ILE D	160	−30.074	43.361	12.218		172.23	H
ATOM	6867	HA	ILE D	160	−31.139	44.990	14.119		186.74	H
ATOM	6868	HB	ILE D	160	−32.571	43.650	12.074		188.02	H
ATOM	6869	HG12	ILE D	160	−32.255	46.450	12.168		171.69	H
ATOM	6870	HG13	ILE D	160	−31.229	45.551	11.355		171.69	H
ATOM	6871	HG21	ILE D	160	−33.883	43.961	13.974		102.016	H
ATOM	6872	HG22	ILE D	160	−33.555	45.516	13.952		102.016	H
ATOM	6873	HG23	ILE D	160	−34.430	44.872	12.793		102.016	H
ATOM	6874	HD11	ILE D	160	−32.806	46.440	9.932		177.27	H
ATOM	6875	HD12	ILE D	160	−32.939	44.857	9.964		177.27	H
ATOM	6876	HD13	ILE D	160	−33.965	45.757	10.778		177.27	H
ATOM	6877	N	PRO D	161	−31.256	43.117	15.758		191.91	N
ATOM	6878	CA	PRO D	161	−31.459	41.971	16.655		100.819	C
ATOM	6879	C	PRO D	161	−32.918	41.531	16.773		107.618	C
ATOM	6880	O	PRO D	161	−33.184	40.448	17.295		110.218	O
ATOM	6881	CB	PRO D	161	−30.946	42.484	18.008		104.117	C
ATOM	6882	CG	PRO D	161	−30.073	43.643	17.685		192.23	C
ATOM	6883	CD	PRO D	161	−30.672	44.267	16.470		190.01	C
ATOM	6884	HA	PRO D	161	−30.917	41.218	16.370		121.017	H
ATOM	6885	HB2	PRO D	161	−31.696	42.763	18.557		125.010	H
ATOM	6886	HB3	PRO D	161	−30.439	41.786	18.451		125.010	H
ATOM	6887	HG2	PRO D	161	−30.073	44.268	18.426		110.618	H
ATOM	6888	HG3	PRO D	161	−29.173	43.331	17.500		110.618	H
ATOM	6889	HD2	PRO D	161	−31.365	44.898	16.720		108.011	H
ATOM	6890	HD3	PRO D	161	−29.984	44.687	15.930		108.011	H
ATOM	6891	N	THR D	162	−33.845	42.358	16.298		107.812	N
ATOM	6892	CA	THR D	162	−35.265	42.042	16.398		113.312	C
ATOM	6893	C	THR D	162	−35.606	40.838	15.526		113.812	C
ATOM	6894	O	THR D	162	−36.327	39.935	15.953		117.217	O
ATOM	6895	CB	THR D	162	−36.158	43.231	15.977		116.015	C
ATOM	6896	OG1	THR D	162	−36.171	43.348	14.549		118.614	O
ATOM	6897	CG2	THR D	162	−35.669	44.537	16.597		119.318	C
ATOM	6898	H	THR D	162	−33.677	43.109	15.914		129.319	H
ATOM	6899	HA	THR D	162	−35.476	41.818	17.318		135.918	H
ATOM	6900	HB	THR D	162	−37.063	43.072	16.288		139.217	H
ATOM	6901	HG1	THR D	162	−36.656	43.994	14.318		142.316	H
ATOM	6902	HG21	THR D	162	−36.242	45.270	16.321		143.216	H
ATOM	6903	HG22	THR D	162	−35.687	44.471	17.565		143.216	H
ATOM	6904	HG23	THR D	162	−34.761	44.721	16.310		143.216	H
ATOM	6905	N	ASN D	163	−35.079	40.834	14.305		109.719	N
ATOM	6906	CA	ASN D	163	−35.341	39.764	13.348		106.911	C
ATOM	6907	C	ASN D	163	−34.070	39.304	12.634		199.24	C
ATOM	6908	O	ASN D	163	−34.132	38.638	11.599		196.09	O
ATOM	6909	CB	ASN D	163	−36.389	40.223	12.329		110.719	C
ATOM	6910	CG	ASN D	163	−36.099	41.606	11.774		109.316	C
ATOM	6911	OD1	ASN D	163	−34.944	41.980	11.575		198.35	O
ATOM	6912	ND2	ASN D	163	−37.154	42.377	11.533		116.018	N
ATOM	6913	H	ASN D	163	−34.559	41.449	14.003		131.715	H
ATOM	6914	HA	ASN D	163	−35.705	39.001	13.824		128.219	H
ATOM	6915	HB2	ASN D	163	−36.404	39.599	11.587		132.915	H
ATOM	6916	HB3	ASN D	163	−37.258	40.249	12.759		132.915	H
ATOM	6917	HD21	ASN D	163	−37.044	43.170	11.218		139.219	H
ATOM	6918	HD22	ASN D	163	−37.947	42.084	11.692		139.219	H
ATOM	6919	N	GLY D	164	−32.918	39.661	13.195		196.98	N
ATOM	6920	CA	GLY D	164	−31.634	39.227	12.670		187.96	C
ATOM	6921	C	GLY D	164	−31.365	39.684	11.248		179.64	C
ATOM	6922	O	GLY D	164	−30.536	39.102	10.548		169.70	O
ATOM	6923	H	GLY D	164	−32.856	40.162	13.892		116.317	H
ATOM	6924	HA2	GLY D	164	−30.926	39.570	13.237		105.516	H
ATOM	6925	HA3	GLY D	164	−31.595	38.258	12.689		105.516	H
ATOM	6926	N	SER D	165	−32.062	40.732	10.822		181.83	N
ATOM	6927	CA	SER D	165	−31.935	41.238	9.460		171.12	C
ATOM	6928	C	SER D	165	−30.735	42.170	9.313		157.71	C
ATOM	6929	O	SER D	165	−30.340	42.844	10.265		155.24	O
ATOM	6930	CB	SER D	165	−33.213	41.973	9.050		173.02	C
ATOM	6931	OG	SER D	165	−33.077	42.556	7.766		171.30	O
ATOM	6932	H	SER D	165	−32.620	41.171	11.307		198.19	H
ATOM	6933	HA	SER D	165	−31.810	40.491	8.855		185.34	H
ATOM	6934	HB2	SER D	165	−33.948	41.341	9.033		187.63	H
ATOM	6935	HB3	SER D	165	−33.394	42.674	9.696		187.63	H
ATOM	6936	HG	SER D	165	−33.785	42.955	7.555		185.56	H
ATOM	6937	N	TRP D	166	−30.159	42.193	8.114		141.62	N
ATOM	6938	CA	TRP D	166	−29.122	43.161	7.768		141.01	C
ATOM	6939	C	TRP D	166	−29.709	44.238	6.867		135.15	C
ATOM	6940	O	TRP D	166	−30.344	43.933	5.858		133.29	O
ATOM	6941	CB	TRP D	166	−27.942	42.481	7.067		131.04	C
ATOM	6942	CG	TRP D	166	−27.138	41.590	7.958		132.96	C
ATOM	6943	CD1	TRP D	166	−27.222	40.232	8.050		139.24	C
ATOM	6944	CD2	TRP D	166	−26.124	41.993	8.889		133.27	C
ATOM	6945	NE1	TRP D	166	−26.324	39.763	8.979		136.80	N
ATOM	6946	CE2	TRP D	166	−25.639	40.824	9.509		132.66	C
ATOM	6947	CE3	TRP D	166	−25.582	43.227	9.257		132.29	C
ATOM	6948	CZ2	TRP D	166	−24.637	40.854	10.475		131.08	C
ATOM	6949	CZ3	TRP D	166	−24.586	43.254	10.217		129.48	C
ATOM	6950	CH2	TRP D	166	−24.125	42.074	10.815		129.86	C
ATOM	6951	H	TRP D	166	−30.355	41.652	7.476		149.94	H
ATOM	6952	HA	TRP D	166	−28.795	43.584	8.577		149.21	H
ATOM	6953	HB2	TRP D	166	−28.282	41.940	6.337		137.24	H
ATOM	6954	HB3	TRP D	166	−27.349	43.165	6.720		137.24	H
ATOM	6955	HD1	TRP D	166	−27.803	39.700	7.556		147.09	H
ATOM	6956	HE1	TRP D	166	−26.212	38.938	9.194		144.16	H
ATOM	6957	HE3	TRP D	166	−25.883	44.014	8.865		138.74	H
ATOM	6958	HZ2	TRP D	166	−24.328	40.072	10.873		137.29	H
ATOM	6959	HZ3	TRP D	166	−24.218	44.069	10.470		135.37	H
ATOM	6960	HH2	TRP D	166	−23.455	42.123	11.457		135.83	H
ATOM	6961	N	GLN D	167	−29.503	45.497	7.238		134.74	N
ATOM	6962	CA	GLN D	167	−29.909	46.611	6.392		136.36	C
ATOM	6963	C	GLN D	167	−28.873	47.728	6.465		132.14	C
ATOM	6964	O	GLN D	167	−27.979	47.711	7.315		128.97	O
ATOM	6965	CB	GLN D	167	−31.294	47.127	6.800		143.23	C
ATOM	6966	CG	GLN D	167	−31.323	47.983	8.059		142.74	C
ATOM	6967	CD	GLN D	167	−32.719	48.487	8.383		145.63	C
ATOM	6968	OE1	GLN D	167	−33.717	47.883	7.991		148.25	O
ATOM	6969	NE2	GLN D	167	−32.795	49.599	9.102		146.85	N
ATOM	6970	H	GLN D	167	−29.130	45.732	7.976		141.69	H
ATOM	6971	HA	GLN D	167	−29.960	46.308	5.472		143.63	H
ATOM	6972	HB2	GLN D	167	−31.649	47.663	6.074		151.88	H
ATOM	6973	HB3	GLN D	167	−31.874	46.364	6.953		151.88	H
ATOM	6974	HG2	GLN D	167	−31.012	47.454	8.810		151.28	H
ATOM	6975	HG3	GLN D	167	−30.747	48.753	7.932		151.28	H
ATOM	6976	HE21	GLN D	167	−33.563	49.925	9.312		156.22	H
ATOM	6977	HE22	GLN D	167	−32.076	49.994	9.360		156.22	H
ATOM	6978	N	TRP D	168	−28.992	48.694	5.561		129.94	N
ATOM	6979	CA	TRP D	168	−28.064	49.813	5.524		127.82	C
ATOM	6980	C	TRP D	168	−28.475	50.864	6.546		133.11	C
ATOM	6981	O	TRP D	168	−29.618	50.874	7.009		132.83	O
ATOM	6982	CB	TRP D	168	−28.007	50.400	4.117		127.85	C
ATOM	6983	CG	TRP D	168	−27.611	49.378	3.104		129.12	C
ATOM	6984	CD1	TRP D	168	−28.412	48.801	2.163		127.50	C
ATOM	6985	CD2	TRP D	168	−26.317	48.788	2.946		122.83	C
ATOM	6986	NE1	TRP D	168	−27.694	47.894	1.423		127.86	N
ATOM	6987	CE2	TRP D	168	−26.404	47.868	1.882		121.96	C
ATOM	6988	CE3	TRP D	168	−25.090	48.953	3.596		124.25	C
ATOM	6989	CZ2	TRP D	168	−25.312	47.116	1.454		118.62	C
ATOM	6990	CZ3	TRP D	168	−24.008	48.207	3.169		121.72	C
ATOM	6991	CH2	TRP D	168	−24.127	47.296	2.111		118.99	C
ATOM	6992	H	TRP D	168	−29.604	48.723	4.958		135.93	H
ATOM	6993	HA	TRP D	168	−27.176	49.498	5.755		133.38	H
ATOM	6994	HB2	TRP D	168	−28.884	50.740	3.877		133.42	H
ATOM	6995	HB3	TRP D	168	−27.354	51.116	4.096		133.42	H
ATOM	6996	HD1	TRP D	168	−29.313	48.995	2.041		133.00	H
ATOM	6997	HE1	TRP D	168	−28.004	47.421	0.775		133.44	H
ATOM	6998	HE3	TRP D	168	−25.004	49.554	4.301		129.10	H
ATOM	6999	HZ2	TRP D	168	−25.387	46.512	0.750		122.35	H
ATOM	7000	HZ3	TRP D	168	−23.188	48.308	3.595		126.06	H
ATOM	7001	HH2	TRP D	168	−23.381	46.810	1.845		122.79	H
ATOM	7002	N	GLU D	169	−27.541	51.742	6.905		132.76	N
ATOM	7003	CA	GLU D	169	−27.781	52.721	7.962		134.47	C
ATOM	7004	C	GLU D	169	−28.861	53.734	7.566		129.80	C
ATOM	7005	O	GLU D	169	−29.420	54.412	8.425		139.17	O
ATOM	7006	CB	GLU D	169	−26.473	53.442	8.329		136.50	C
ATOM	7007	CG	GLU D	169	−25.907	54.339	7.239		137.04	C
ATOM	7008	CD	GLU D	169	−24.412	54.619	7.405		137.98	C
ATOM	7009	OE1	GLU D	169	−23.995	55.125	8.473		134.25	O
ATOM	7010	OE2	GLU D	169	−23.651	54.335	6.457		131.91	O1−
ATOM	7011	H	GLU D	169	−26.759	51.790	6.551		139.31	H
ATOM	7012	HA	GLU D	169	−28.091	52.254	8.753		141.37	H
ATOM	7013	HB2	GLU D	169	−26.634	53.996	9.109		143.80	H
ATOM	7014	HB3	GLU D	169	−25.800	52.775	8.537		143.80	H
ATOM	7015	HG2	GLU D	169	−26.036	53.909	6.379		144.45	H
ATOM	7016	HG3	GLU D	169	−26.374	55.189	7.256		144.45	H
ATOM	7017	N	ASP D	170	−29.163	53.822	6.273		130.55	N
ATOM	7018	CA	ASP D	170	−30.212	54.719	5.789		131.25	C
ATOM	7019	C	ASP D	170	−31.587	54.053	5.821		131.67	C
ATOM	7020	O	ASP D	170	−32.580	54.645	5.407		137.31	O
ATOM	7021	CB	ASP D	170	−29.900	55.192	4.366		125.76	C
ATOM	7022	CG	ASP D	170	−30.035	54.083	3.334		129.56	C
ATOM	7023	OD1	ASP D	170	−30.204	52.907	3.720		130.98	O
ATOM	7024	OD2	ASP D	170	−29.959	54.387	2.127		127.01	O1−
ATOM	7025	H	ASP D	170	−28.774	53.372	5.652		136.66	H
ATOM	7026	HA	ASP D	170	−30.246	55.501	6.362		137.50	H
ATOM	7027	HB2	ASP D	170	−30.517	55.901	4.127		130.92	H
ATOM	7028	HB3	ASP D	170	−28.988	55.521	4.335		130.92	H
ATOM	7029	N	GLY D	171	−31.629	52.808	6.286		131.62	N
ATOM	7030	CA	GLY D	171	−32.877	52.081	6.423		131.76	C
ATOM	7031	C	GLY D	171	−33.213	51.178	5.248		132.34	C
ATOM	7032	O	GLY D	171	−34.017	50.259	5.393		136.75	O
ATOM	7033	H	GLY D	171	−30.937	52.361	6.531		137.95	H
ATOM	7034	HA2	GLY D	171	−32.836	51.532	7.221		138.11	H
ATOM	7035	HA3	GLY D	171	−33.603	52.715	6.531		138.11	H
ATOM	7036	N	SER D	172	−32.609	51.426	4.088		129.62	N
ATOM	7037	CA	SER D	172	−32.938	50.654	2.888		131.61	C
ATOM	7038	C	SER D	172	−32.552	49.188	3.061		130.37	C
ATOM	7039		SER D	172	−31.747	48.846	3.927		133.60	O
ATOM	7040	CB	SER D	172	−32.246	51.240	1.650		133.37	C
ATOM	7041	OG	SER D	172	−30.837	51.125	1.737		130.18	O
ATOM	7042	H	SER D	172	−32.009	52.031	3.968		135.54	H
ATOM	7043	HA	SER D	172	−33.895	50.696	2.742		137.93	H
ATOM	7044	HB2	SER D	172	−32.552	50.761	0.864		140.04	H
ATOM	7045	HB3	SER D	172	−32.479	52.179	1.576		140.04	H
ATOM	7046	HG	SER D	172	−30.619	50.316	1.800		136.22	H
ATOM	7047	N	ILE D	173	−33.139	48.325	2.236		134.65	N
ATOM	7048	CA	ILE D	173	−32.919	46.889	2.352		135.81	C
ATOM	7049	C	ILE D	173	−31.672	46.444	1.600		132.48	C
ATOM	7050	O	ILE D	173	−31.201	47.117	0.676		125.43	O
ATOM	7051	CB	ILE D	173	−34.131	46.073	1.827		136.56	C
ATOM	7052	CG1	ILE D	173	−34.365	46.330	0.332		138.02	C
ATOM	7053	CG2	ILE D	173	−35.382	46.407	2.633		143.13	C
ATOM	7054	CD1	ILE D	173	−35.348	45.372	−0.303		140.93	C
ATOM	7055	H	ILE D	173	−33.671	48.548	1.598		141.58	H
ATOM	7056	HA	ILE D	173	−32.796	46.667	3.289		142.97	H
ATOM	7057	HB	ILE D	173	−33.936	45.130	1.945		143.88	H
ATOM	7058	HG12	ILE D	173	−34.713	47.229	0.220		145.63	H
ATOM	7059	HG13	ILE D	173	−33.521	46.243	−0.137		145.63	H
ATOM	7060	HG21	ILE D	173	−36.126	45.888	2.289		151.76	H
ATOM	7061	HG22	ILE D	173	−35.225	46.186	3.564		151.76	H
ATOM	7062	HG23	ILE D	173	−35.570	47.355	2.544		151.76	H
ATOM	7063	HD11	ILE D	173	−35.444	45.595	−1.242		149.11	H
ATOM	7064	HD12	ILE D	173	−35.010	44.467	−0.211		149.11	H
ATOM	7065	HD13	ILE D	173	−36.203	45.453	0.147		149.11	H
ATOM	7066	N	LEU D	174	−31.153	45.293	2.007		131.77	N
ATOM	7067	CA	LEU D	174	−30.037	44.657	1.330		127.52	C
ATOM	7068	C	LEU D	174	−30.557	43.827	0.166		125.72	C
ATOM	7069	O	LEU D	174	−31.252	42.838	0.374		130.63	O
ATOM	7070	CB	LEU D	174	−29.257	43.784	2.312		131.85	C
ATOM	7071	CG	LEU D	174	−28.071	42.986	1.764		133.37	C
ATOM	7072	CD1	LEU D	174	−27.043	43.905	1.129		126.92	C
ATOM	7073	CD2	LEU D	174	−27.441	42.169	2.880		126.89	C
ATOM	7074	H	LEU D	174	−31.438	44.853	2.688		138.12	H
ATOM	7075	HA	LEU D	174	−29.440	45.337	0.980		133.02	H
ATOM	7076	HB2	LEU D	174	−28.912	44.357	3.015		138.22	H
ATOM	7077	HB3	LEU D	174	−29.874	43.144	2.700		138.22	H
ATOM	7078	HG	LEU D	174	−28.389	42.372	1.084		140.04	H
ATOM	7079	HD11	LEU D	174	−26.307	43.370	0.793		132.31	H
ATOM	7080	HD12	LEU D	174	−27.461	44.389	0.400		132.31	H
ATOM	7081	HD13	LEU D	174	−26.721	44.528	1.799		132.31	H
ATOM	7082	HD21	LEU D	174	−26.692	41.669	2.521		132.27	H
ATOM	7083	HD22	LEU D	174	−27.134	42.771	3.577		132.27	H
ATOM	7084	HD23	LEU D	174	−28.105	41.559	3.239		132.27	H
ATOM	7085	N	SER D	175	−30.242	44.239	−1.058		127.73	N
ATOM	7086	CA	SER D	175	−30.653	43.479	−2.231		123.91	C
ATOM	7087	C	SER D	175	−30.187	42.029	−2.083		128.76	C
ATOM	7088	O	SER D	175	−28.991	41.786	−1.925		127.41	O
ATOM	7089	CB	SER D	175	−30.077	44.098	−3.505		126.73	C
ATOM	7090	OG	SER D	175	−30.445	43.344	−4.648		122.87	O
ATOM	7091	H	SER D	175	−29.793	44.951	−1.234		133.27	H
ATOM	7092	HA	SER D	175	−31.620	43.485	−2.297		128.69	H
ATOM	7093	HB2	SER D	175	−30.419	45.000	−3.600		132.07	H
ATOM	7094	HB3	SER D	175	−29.110	44.116	−3.438		132.07	H
ATOM	7095	HG	SER D	175	−30.123	43.694	−5.340		127.44	H
ATOM	7096	N	PRO D	176	−31.127	41.063	−2.098		125.88	N
ATOM	7097	CA	PRO D	176	−30.728	39.659	−1.923		127.19	C
ATOM	7098	C	PRO D	176	−29.657	39.204	−2.916		126.97	C
ATOM	7099	O	PRO D	176	−29.693	39.601	−4.079		127.85	O
ATOM	7100	CB	PRO D	176	−32.035	38.891	−2.155		123.99	C
ATOM	7101	CG	PRO D	176	−33.107	39.860	−1.828		125.30	C
ATOM	7102	CD	PRO D	176	−32.588	41.204	−2.234		125.95	C
ATOM	7103	HA	PRO D	176	−30.418	39.504	−1.017		132.63	H
ATOM	7104	HB2	PRO D	176	−32.092	38.614	−3.082		128.78	H
ATOM	7105	HB3	PRO D	176	−32.073	38.123	−1.563		128.78	H
ATOM	7106	HG2	PRO D	176	−33.907	39.638	−2.330		130.36	H
ATOM	7107	HG3	PRO D	176	−33.285	39.837	−0.875		130.36	H
ATOM	7108	HD2	PRO D	176	−32.825	41.393	−3.155		131.14	H
ATOM	7109	HD3	PRO D	176	−32.919	41.889	−1.633		131.14	H
ATOM	7110	N	ASN D	177	−28.715	38.392	−2.442		124.96	N
ATOM	7111	CA	ASN D	177	−27.667	37.810	−3.280		124.54	C
ATOM	7112	C	ASN D	177	−26.704	38.844	−3.866		129.77	C
ATOM	7113	O	ASN D	177	−26.083	38.603	−4.900		133.58	O
ATOM	7114	CB	ASN D	177	−28.291	36.990	−4.415		130.08	C
ATOM	7115	CG	ASN D	177	−29.188	35.884	−3.905		129.31	C
ATOM	7116	OD1	ASN D	177	−30.398	35.883	−4.142		127.98	O
ATOM	7117	ND2	ASN D	177	−28.598	34.933	−3.193		130.03	N
ATOM	7118	H	ASN D	177	−28.660	38.158	−1.616		129.95	H
ATOM	7119	HA	ASN D	177	−27.144	37.202	−2.735		129.44	H
ATOM	7120	HB2	ASN D	177	−28.825	37.576	−4.974		136.09	H
ATOM	7121	HB3	ASN D	177	−27.583	36.585	−4.940		136.09	H
ATOM	7122	HD21	ASN D	177	−29.062	34.281	−2.879		136.03	H
ATOM	7123	HD22	ASN D	177	−27.752	34.969	−3.046		136.03	H
ATOM	7124	N	LEU D	178	−26.577	39.988	−3.202		129.98	N
ATOM	7125	CA	LEU D	178	−25.592	40.989	−3.594		125.52	C
ATOM	7126	C	LEU D	178	−24.290	40.721	−2.851		126.67	C
ATOM	7127	O	LEU D	178	−23.228	40.588	−3.463		128.33	O
ATOM	7128	CB	LEU D	178	−26.098	42.400	−3.295		126.47	C
ATOM	7129	CG	LEU D	178	−25.654	43.482	−4.281		126.81	C
ATOM	7130	CD1	LEU D	178	−26.117	44.846	−3.805		126.04	C
ATOM	7131	CD2	LEU D	178	−24.150	43.470	−4.484		128.87	C
ATOM	7132	H	LEU D	178	−27.051	40.209	−2.520		135.97	H
ATOM	7133	HA	LEU D	178	−25.423	40.919	−4.546		130.62	H
ATOM	7134	HB2	LEU D	178	−27.068	42.385	−3.298		131.77	H
ATOM	7135	HB3	LEU D	178	−25.781	42.659	−2.416		131.77	H
ATOM	7136	HG	LEU D	178	−26.070	43.312	−5.141		132.18	H
ATOM	7137	HD11	LEU D	178	−25.727	45.025	−2.934		131.25	H
ATOM	7138	HD12	LEU D	178	−25.826	45.518	−4.442		131.25	H
ATOM	7139	HD13	LEU D	178	−27.085	44.847	−3.741		131.25	H
ATOM	7140	HD21	LEU D	178	−23.910	44.168	−5.113		134.64	H
ATOM	7141	HD22	LEU D	178	−23.716	43.630	−3.631		134.64	H
ATOM	7142	HD23	LEU D	178	−23.885	42.605	−4.833		134.64	H
ATOM	7143	N	LEU D		179	−24.389	40.630	−1.528		119.13	N
ATOM	7144	CA	LEU D	179	−23.244	40.332	−0.679		121.55	C
ATOM	7145	C	LEU D	179	−23.321	38.920	−0.113		128.27	C
ATOM	7146	O	LEU D	179	−24.408	38.392	0.125		125.28	O
ATOM	7147	CB	LEU D	179	−23.155	41.335	0.469		122.39	C
ATOM	7148	CG	LEU D		179	−22.856	42.788	0.096		122.47	C
ATOM	7149	CD1	LEU D	179	−22.901	43.661	1.336		124.98	C
ATOM	7150	CD2	LEU D	179	−21.504	42.910	−0.586		123.45	C
ATOM	7151	H	LEU D		179	−25.123	40.739	−1.093		122.95	H
ATOM	7152	HA	LEU D		179	−22.432	40.403	−1.205		125.86	H
ATOM	7153	HB2	LEU D	179	−24.003	41.329	0.941		126.87	H
ATOM	7154	HB3	LEU D	179	−22.453	41.043	1.071		126.87	H
ATOM	7155	HG	LEU D	179	−23.535	43.104	−0.521		126.97	H
ATOM	7156	HD11	LEU D	179	−22.710	44.577	1.083		129.97	H
ATOM	7157	HD12	LEU D	179	−23.786	43.604	1.729		129.97	H
ATOM	7158	HD13	LEU D	179	−22.237	43.346	1.968		129.97	H
ATOM	7159	HD21	LEU D	179	−21.346	43.840	−0.809		128.13	H
ATOM	7160	HD22	LEU D	179	−20.816	42.593	0.020		128.13	H
ATOM	7161	HD23	LEU D	179	−21.508	42.372	−1.393		128.13	H
ATOM	7162	N	THR D	180	−22.153	38.316	0.088		119.72	N
ATOM	7163	CA	THR D	180	−22.040	37.069	0.827		119.71	C
ATOM	7164	C	THR D	180	−21.583	37.388	2.242		123.17	C
ATOM	7165	O	THR D	180	−20.446	37.813	2.455		123.15	O
ATOM	7166	CB	THR D	180	−21.059	36.099	0.154		123.54	C
ATOM	7167	OG1	THR D	180	−21.581	35.709	−1.122		125.00	O
ATOM	7168	CG2	THR D	180	−20.847	34.854	1.006		124.90	C
ATOM	7169	H	THR D	180	−21.401	38.616	−0.201		123.66	H
ATOM	7170	HA	THR D	180	−22.910	36.642	0.875		123.65	H
ATOM	7171	HB	THR D	180	−20.203	36.538	0.032		128.24	H
ATOM	7172	HG1	THR D	180	−21.682	36.386	−1.610		130.00	H
ATOM	7173	HG21	THR D	180	−20.225	34.253	0.566		129.88	H
ATOM	7174	HG22	THR D	180	−20.486	35.102	1.872		129.88	H
ATOM	7175	HG23	THR D	180	−21.691	34.394	1.137		129.88	H
ATOM	7176	N	ILE D	181	−22.478	37.187	3.204		122.44	N
ATOM	7177	CA	ILE D	181	−22.186	37.469	4.602		123.18	C
ATOM	7178	C	ILE D	181	−21.541	36.264	5.269		125.41	C
ATOM	7179	O	ILE D	181	−22.102	35.168	5.252		123.82	O
ATOM	7180	CB	ILE D	181	−23.459	37.851	5.386		125.11	C
ATOM	7181	CG1	ILE D	181	−24.171	39.037	4.725		125.99	C
ATOM	7182	CG2	ILE D	181	−23.116	38.174	6.841		132.01	C
ATOM	7183	CD1	ILE D	181	−23.360	40.323	4.695		129.24	C
ATOM	7184	H	ILE D	181	−23.271	36.883	3.069		126.93	H
ATOM	7185	HA	ILE D	181	−21.565	38.212	4.654		127.81	H
ATOM	7186	HB	ILE D	181	−24.062	37.091	5.377		130.13	H
ATOM	7187	HG12	ILE D	181	−24.382	38.800	3.809		131.19	H
ATOM	7188	HG13	ILE D	181	−24.990	39.218	5.213		131.19	H
ATOM	7189	HG21	ILE D	181	−23.930	38.411	7.312		138.41	H
ATOM	7190	HG22	ILE D	181	−22.711	37.393	7.250		138.41	H
ATOM	7191	HG23	ILE D	181	−22.494	38.918	6.861		138.41	H
ATOM	7192	HD11	ILE D	181	−23.883	41.016	4.262		135.08	H
ATOM	7193	HD12	ILE D	181	−23.151	40.586	5.605		135.08	H
ATOM	7194	HD13	ILE D	181	−22.541	40.168	4.198		135.08	H
ATOM	7195	N	ILE D	182	−20.375	36.484	5.873		123.72	N
ATOM	7196	CA	ILE D	182	−19.615	35.416	6.521		122.37	C
ATOM	7197	C	ILE D	182	−19.531	35.640	8.024		122.69	C
ATOM	7198	O	ILE D	182	−19.146	36.717	8.478		117.58	O
ATOM	7199	CB	ILE D	182	−18.184	35.315	5.950		120.91	C
ATOM	7200	CG1	ILE D	182	−18.233	35.144	4.428		119.30	C
ATOM	7201	CG2	ILE D	182	−17.422	34.159	6.609		118.99	C
ATOM	7202	CD1	ILE D	182	−16.890	35.250	3.753		120.70	C
ATOM	7203	H	ILE D	182	−19.997	37.255	5.922		128.47	H
ATOM	7204	HA	ILE D	182	−20.062	34.569	6.366		126.85	H
ATOM	7205	HB	ILE D	182	−17.716	36.141	6.149		125.09	H
ATOM	7206	HG12	ILE D	182	−18.598	34.269	4.225		123.16	H
ATOM	7207	HG13	ILE D	182	−18.805	35.833	4.056		123.16	H
ATOM	7208	HG21	ILE D	182	−16.528	34.116	6.235		122.78	H
ATOM	7209	HG22	ILE D	182	−17.373	34.318	7.565		122.78	H
ATOM	7210	HG23	ILE D	182	−17.894	33.330	6.435		122.78	H
ATOM	7211	HD11	ILE D	182	−17.007	35.131	2.797		124.84	H
ATOM	7212	HD12	ILE D	182	−16.513	36.125	3.934		124.84	H
ATOM	7213	HD13	ILE D	182	−16.305	34.559	4.103		124.84	H
ATOM	7214	N	GLU D	183	−19.895	34.615	8.789		124.20	N
ATOM	7215	CA	GLU D	183	−19.788	34.661	10.241		126.38	C
ATOM	7216	C	GLU D	183	−18.337	34.472	10.651		131.18	C
ATOM	7217	O	GLU D	183	−17.673	33.538	10.205		129.96	O
ATOM	7218	CB	GLU D	183	−20.662	33.587	10.888		135.36	C
ATOM	7219	CG	GLU D	183	−22.150	33.765	10.648		146.80	C
ATOM	7220	CD	GLU D	183	−22.982	32.679	11.304		173.69	C
ATOM	7221	OE1	GLU D	183	−22.398	31.680	11.776		179.19	O
ATOM	7222	OE2	GLU D	183	−24.222	32.825	11.351		181.50	O1−
ATOM	7223	H	GLU D	183	−20.210	33.874	8.486		129.04	H
ATOM	7224	HA	GLU D	183	−20.085	35.529	10.557		131.66	H
ATOM	7225	HB2	GLU D	183	−20.407	32.722	10.531		142.43	H
ATOM	7226	HB3	GLU D	183	−20.514	33.602	11.847		142.43	H
ATOM	7227	HG2	GLU D	183	−22.430	34.619	11.013		156.15	H
ATOM	7228	HG3	GLU D	183	−22.322	33.739	9.694		156.15	H
ATOM	7229	N	MET D	184	−17.846	35.363	11.502		130.31	N
ATOM	7230	CA	MET D	184	−16.458	35.313	11.938		129.78	C
ATOM	7231	C	MET D	184	−16.376	35.603	13.430		135.79	C
ATOM	7232	O	MET D	184	−16.026	34.731	14.229		137.59	O
ATOM	7233	CB	MET D	184	−15.621	36.315	11.147		127.05	C
ATOM	7234	CG	MET D	184	−14.138	36.253	11.442		126.53	C
ATOM	7235	SD	MET D	184	−13.261	37.651	10.735		130.02	S
ATOM	7236	CE	MET D	184	−13.846	38.985	11.783		131.51	C
ATOM	7237	I	MET D	184	−18.299	36.010	11.843		136.37	H
ATOM	7238	HA	MET D	184	−16.104	34.426	11.768		135.73	H
ATOM	7239	HB2	MET D	184	−15.741	36.142	10.200		132.46	H
ATOM	7240	HB3	MET D	184	−15.927	37.211	11.357		132.46	H
ATOM	7241	HG2	MET D	184	−14.002	36.265	12.403		131.83	H
ATOM	7242	HG3	MET D	184	−13.770	35.441	11.062		131.83	H
ATOM	7243	HE1	MET D	184	−13.435	39.816	11.496		137.82	H
ATOM	7244	HE2	MET D	184	−14.811	39.049	11.703		137.82	H
ATOM	7245	HE3	MET D	184	−13.602	38.795	12.702		137.82	H
ATOM	7246	N	GLN D	185	−16.705	36.837	13.791		133.99	N
ATOM	7247	CA	GLN D	185	−16.777	37.246	15.185		137.58	C
ATOM	7248	C	GLN D	185	−18.202	37.678	15.488		140.84	C
ATOM	7249	O	GLN D	185	−18.821	38.383	14.691		136.32	O
ATOM	7250	CB	GLN D	185	−15.797	38.383	15.470		140.17	C
ATOM	7251	CG	GLN D	185	−15.634	38.706	16.944		146.92	C
ATOM	7252	CD	GLN D	185	−14.883	37.625	17.695		155.70	C
ATOM	7253	OE1	GLN D	185	−13.773	37.249	17.317		153.14	O
ATOM	7254	NE2	GLN D	185	−15.487	37.116	18.763		159.98	N
ATOM	7255	H	GLN D	185	−16.894	37.467	13.236		140.79	H
ATOM	7256	HA	GLN D	185	−16.554	36.495	15.756		145.09	H
ATOM	7257	HB2	GLN D	185	−14.925	38.137	15.124		148.21	H
ATOM	7258	HB3	GLN D	185	−16.111	39.185	15.025		148.21	H
ATOM	7259	HG2	GLN D	185	−15.139	39.535	17.034		156.30	H
ATOM	7260	HG3	GLN D	185	−16.512	38.797	17.347		156.30	H
ATOM	7261	HE21	GLN D	185	−15.101	36.500	19.222		171.97	H
ATOM	7262	HE22	GLN D	185	−16.264	37.402	18.995		171.97	H
ATOM	7263	N	LYS D	186	−18.723	37.242	16.631		146.47	N
ATOM	7264	CA	LYS D	186	−20.057	37.639	17.061		145.40	C
ATOM	7265	C	LYS D	186	−20.143	39.158	17.171		139.69	C
ATOM	7266	O	LYS D	186	−19.414	39.777	17.947		141.64	O
ATOM	7267	CB	LYS D	186	−20.405	36.981	18.398		151.52	C
ATOM	7268	CG	LYS D	186	−20.680	35.489	18.289		165.11	C
ATOM	7269	CD	LYS D	186	−19.861	34.683	19.288		184.25	C
ATOM	7270	CE	LYS D	186	−20.168	33.195	19.180		186.61	C
ATOM	7271	NZ	LYS D	186	−18.935	32.360	19.163		176.57	N1+
ATOM	7272	H	LYS D	186	−18.321	36.712	17.176		155.77	H
ATOM	7273	HA	LYS D	186	−20.705	37.346	16.402		154.47	H
ATOM	7274	HB2	LYS D	186	−19.662	37.103	19.010		161.82	H
ATOM	7275	HB3	LYS D	186	−21.200	37.405	18.758		161.82	H
ATOM	7276	HG2	LYS D	186	−21.619	35.325	18.466		178.14	H
ATOM	7277	HG3	LYS D	186	−20.450	35.188	17.397		178.14	H
ATOM	7278	HD2	LYS D	186	−18.917	34.814	19.108		101.110	H
ATOM	7279	HD3	LYS D	186	−20.076	34.975	20.188		101.110	H
ATOM	7280	HE2	LYS D	186	20.703	32.926	19.943		103.914	H
ATOM	7281	HE3	LYS D	186	−20.654	33.031	18.357		103.914	H
ATOM	7282	HZ1	LYS D	186	−19.151	31.500	19.100		191.88	H
ATOM	7283	HZ2	LYS D	186	−18.426	32.583	18.467		191.88	H
ATOM	7284	HZ3	LYS D	186	−18.471	32.488	19.912		191.88	H
ATOM	7285	N	GLY D	187	−21.027	39.755	16.379		138.31	N
ATOM	7286	CA	GLY D	187	−21.164	41.200	16.353		135.66	C
ATOM	7287	C	GLY D	187	−22.311	41.654	15.477		129.40	C
ATOM	7288	O	GLY D	187	−22.977	40.839	14.843		128.79	O
ATOM	7289	H	GLY D	187	−21.560	39.342	15.845		145.97	H
ATOM	7290	HA2	GLY D	187	−21.318	41.526	17.254		142.79	H
ATOM	7291	HA3	GLY D	187	−20.345	41.596	16.018		142.79	H
ATOM	7292	N	ASP D	188	−22.528	42.966	15.435		130.44	N
ATOM	7293	CA	ASP D	188	−23.660	43.549	14.722		129.39	C
ATOM	7294	C	ASP D	188	−23.208	44.460	13.580		129.72	C
ATOM	7295	O	ASP D	188	−24.003	45.223	13.031		131.13	O
ATOM	7296	CB	ASP D	188	−24.540	44.327	15.705		137.77	C
ATOM	7297	CG	ASP D	188	−25.117	43.439	16.801		139.59	C
ATOM	7298	OD1	ASP D	188	−25.551	42.311	16.485		140.77	O
ATOM	7299	OD2	ASP D	188	−25.127	43.863	17.977		138.82	O1−
ATOM	7300	H	ASP D	188	−22.025	43.548	15.819		136.53	H
ATOM	7301	HA	ASP D	188	−24.195	42.835	14.341		135.27	H
ATOM	7302	HB2	ASP D	188	−24.007	45.019	16.128		145.33	H
ATOM	7303	HB3	ASP D	188	−25.280	44.726	15.221		145.33	H
ATOM	7304	N	CYS D	189	−21.928	44.372	13.230		129.33	N
ATOM	7305	CA	CYS D	189	−21.362	45.161	12.140		127.86	C
ATOM	7306	C	CYS D	189	−20.576	44.256	11.195		125.45	C
ATOM	7307	O	CYS D	189	−20.198	43.145	11.568		123.49	O
ATOM	7308	CB	CYS D	189	−20.468	46.272	12.692		128.54	C
ATOM	7309	SG	CYS D	189	−21.349	47.483	13.716		129.86	S
ATOM	7310	H	CYS D	189	−21.358	43.854	13.613		135.19	H
ATOM	7311	HA	CYS D	189	−22.082	45.573	11.637		133.43	H
ATOM	7312	HB2	CYS D	189	−19.773	45.872	13.238		134.24	H
ATOM	7313	HB3	CYS D	189	−20.067	46.749	11.948		134.24	H
ATOM	7314	N	ALA D	190	−20.337	44.731	9.975		122.91	N
ATOM	7315	CA	ALA D	190	−19.680	43.915	8.960		122.33	C
ATOM	7316	C	ALA D	190	−18.577	44.667	8.221		120.44	C
ATOM	7317	O	ALA D	190	−18.711	45.845	7.890		120.09	O
ATOM	7318	CB	ALA D	190	−20.702	43.395	7.971		121.39	C
ATOM	7319	H	ALA D	190	−20.546	45.522	9.710		127.50	H
ATOM	7320	HA	ALA D	190	−19.273	43.149	9.394		126.80	H
ATOM	7321	HB1	ALA D	190	−20.250	42.855	7.304		125.67	H
ATOM	7322	HB2	ALA D	190	−21.355	42.856	8.446		125.67	H
ATOM	7323	HB3	ALA D	190	−21.141	44.148	7.545		125.67	H
ATOM	7324	N	LEU D	191	−17.484	43.959	7.972		117.46	N
ATOM	7325	CA	LEU D	191	−16.381	44.479	7.183		117.75	C
ATOM	7326	C	LEU D	191	−16.573	44.087	5.727		115.67	C
ATOM	7327	O	LEU D	191	−16.806	42.915	5.429		116.92	O
ATOM	7328	CB	LEU D	191	−15.052	43.935	7.699		115.85	C
ATOM	7329	CG	LEU D	191	−14.674	44.331	9.125		117.91	C
ATOM	7330	CD1	LEU D	191	−13.616	43.387	9.665		117.38	C
ATOM	7331	CD2	LEU D	191	−14.181	45.770	9.157		116.48	C
ATOM	7332	H	LEU D	191	−17.356	43.157	8.256		120.95	H
ATOM	7333	HA	LEU D	191	−16.364	45.447	7.244		121.30	H
ATOM	7334	HB2	LEU D	191	−15.087	42.966	7.668		119.03	H
ATOM	7335	HB3	LEU D	191	−14.346	44.251	7.115		119.03	H
ATOM	7336	HG	LEU D	191	−15.458	44.265	9.693		121.50	H
ATOM	7337	HD11	LEU D	191	−13.388	43.652	10.569		120.86	H
ATOM	7338	HD12	LEU D	191	−13.969	42.483	9.664		120.86	H
ATOM	7339	HD13	LEU D	191	−12.830	43.436	9.097		120.86	H
ATOM	7340	HD21	LEU D	191	−13.946	46.003	10.069		119.78	H
ATOM	7341	HD22	LEU D	191	−13.402	45.850	8.584		119.78	H
ATOM	7342	HD23	LEU D	191	−14.888	46.353	8.838		119.78	H
ATOM	7343	N	TYR D	192	−16.495	45.052	4.819		115.37	N
ATOM	7344	CA	TYR D	192	−16.479	44.714	3.406		113.02	C
ATOM	7345	C	TYR D	192	−15.140	44.117	3.025		116.84	C
ATOM	7346	O	TYR D	192	−14.100	44.556	3.500		113.73	O
ATOM	7347	CB	TYR D	192	−16.737	45.919	2.500		114.04	C
ATOM	7348	CG	TYR D	192	−16.606	45.490	1.060		115.73	C
ATOM	7349	CD1	TYR D	192	−17.668	44.878	0.411		115.86	C
ATOM	7350	CD2	TYR D	192	−15.399	45.615	0.376		115.68	C
ATOM	7351	CE1	TYR D	192	−17.553	44.440	−0.884		116.16	C
ATOM	7352	CE2	TYR D	192	−15.272	45.172	−0.928		116.99	C
ATOM	7353	CZ	TYR D	192	−16.358	44.585	−1.552		118.72	C
ATOM	7354	OH	TYR D	192	−16.257	44.134	−2.845		120.02	O
ATOM	7355	H	TYR D	192	−16.451	45.893	4.992		118.45	H
ATOM	7356	HA	TYR D	192	−17.166	44.052	3.231		115.62	H
ATOM	7357	HB2	TYR D	192	−17.637	46.252	2.645		116.85	H
ATOM	7358	HB3	TYR D	192	−16.082	46.611	2.680		116.85	H
ATOM	7359	HD1	TYR D	192	−18.477	44.774	0.858		119.03	H
ATOM	7360	HD2	TYR D	192	−14.670	46.006	0.800		118.82	H
ATOM	7361	HE1	TYR D	192	−18.279	44.042	−1.308		119.40	H
ATOM	7362	HE2	TYR D	192	−14.466	45.270	−1.381		120.39	H
ATOM	7363	HH	TYR D	192	−15.484	44.279	−3.140		124.03	H
ATOM	7364	N	ALA D	193	−15.174	43.130	2.136		116.16	N
ATOM	7365	CA	ALA D	193	−13.962	42.620	1.512		115.91	C
ATOM	7366	O	ALA D	193	−14.293	41.994	0.167		117.11	C
ATOM	7367	O	ALA D	193	−15.458	41.709	−0.137		114.31	O
ATOM	7368	CB	ALA D	193	−13.279	41.614	2.413		117.57	C
ATOM	7369	H	ALA D	193	−15.894	42.736	1.876		119.39	H
ATOM	7370	HA	ALA D	193	−13.349	43.356	1.360		119.09	H
ATOM	7371	HB1	ALA D	193	−12.476	41.292	1.974		121.09	H
ATOM	7372	HB2	ALA D	193	−13.047	42.047	3.250		121.09	H
ATOM	7373	HB3	ALA D	193	−13.885	40.876	2.578		121.09	H
ATOM	7374	N	SER D	194	−13.261	41.795	−0.642		113.16	N
ATOM	7375	CA	SER D	194	−13.424	41.159	−1.940		119.38	C
ATOM	7376	C	SER D	194	−13.783	39.688	−1.736		115.86	C
ATOM	7377	O	SER D	194	−13.257	39.081	−0.811		117.79	O
ATOM	7378	CB	SER D	194	−12.134	41.288	−2.759		116.87	C
ATOM	7379	OG	SER D	194	−12.254	40.631	−4.006		119.40	O
ATOM	7380	H	SER D	194	−12.452	42.020	−0.461		115.79	H
ATOM	7381	HA	SER D	194	−14.144	41.590	−2.427		123.26	H
ATOM	7382	HB2	SER D	194	−11.953	42.228	−2.914		120.25	H
ATOM	7383	HB3	SER D	194	−11.404	40.888	−2.261		120.25	H
ATOM	7384	HG	SER D	194	−11.540	40.711	−4.442		123.28	H
ATOM	7385	N	SER D	195	−14.655	39.097	−2.558		116.08	N
ATOM	7386	CA	SER D	195	−15.382	39.753	−3.644		119.93	C
ATOM	7387	C	SER D	195	−16.864	39.846	−3.286		118.77	C
ATOM	7388	O	SER D	195	−17.570	38.835	−3.271		117.62	O
ATOM	7389	CB	SER D	195	−15.212	38.984	−4.953		117.02	C
ATOM	7390	OG	SER D	195	−15.833	39.680	−6.022		121.30	O
ATOM	7391	H	SER D	195	−14.851	38.262	−2.497		119.30	H
ATOM	7392	HA	SER D	195	−15.037	40.652	−3.768		123.92	H
ATOM	7393	HB2	SER D	195	−14.266	38.888	−5.144		120.43	H
ATOM	7394	HB3	SER D	195	−15.623	38.110	−4.863		120.43	H
ATOM	7395	HG	SER D	195	−15.736	39.252	−6.738		125.57	H
ATOM	7396	N	PHE D	196	−17.323	41.062	−3.010		116.50	N
ATOM	7397	CA	PHE D	196	−18.681	41.297	−2.521		118.66	C
ATOM	7398	C	PHE D	196	−18.989	40.392	−1.338		116.83	C
ATOM	7399	O	PHE D	196	−19.992	39.680	−1.320		117.38	O
ATOM	7400	CB	PHE D	196	−19.699	41.099	−3.646		116.78	C
ATOM	7401	CG	PHE D	196	−19.660	42.189	−4.674		118.16	C
ATOM	7402	CD1	PHE D	196	−18.851	42.083	−5.789		119.31	C
ATOM	7403	CD2	PHE D	196	−20.415	43.336	−4.509		123.49	C
ATOM	7404	CE1	PHE D	196	−18.805	43.095	−6.725		121.60	C
ATOM	7405	CE2	PHE D	196	−20.372	44.349	−5.443		121.99	C
ATOM	7406	CZ	PHE D	196	−19.567	44.230	−6.549		121.26	C
ATOM	7407	H	PHE D	196	−16.860	41.782	−3.098		119.80	H
ATOM	7408	HA	PHE D	196	−18.750	42.215	−2.218		122.39	H
ATOM	7409	HB2	PHE D	196	−19.513	40.259	−4.095		120.13	H
ATOM	7410	HB3	PHE D	196	−20.590	41.080	−3.264		120.13	H
ATOM	7411	HD1	PHE D	196	−18.334	41.320	−5.911		123.17	H
ATOM	7412	HD2	PHE D	196	−20.960	43.423	−3.761		128.18	H
ATOM	7413	HE1	PHE D	196	−18.261	43.011	−7.475		125.93	H
ATOM	7414	HE2	PHE D	196	−20.888	45.114	−5.323		126.39	H
ATOM	7415	HZ	PHE D	196	−19.540	44.911	−7.181		125.51	H
ATOM	7416	N	LYS D		197	−18.103	40.436	−0.351		114.08	N
ATOM	7417	CA	LYS D	197	−18.266	39.684	0.880		114.96	C
ATOM	7418	C	LYS D	197	−18.416	40.637	2.051		118.83	C
ATOM	7419	O	LYS D	197	−17.959	41.781	2.004		117.01	O
ATOM	7420	CB	LYS D	197	−17.076	38.744	1.114		117.88	C
ATOM	7421	CG	LYS D	197	−17.105	37.490	0.254		116.95	C
ATOM	7422	CD	LYS D	197	−15.837	36.661	0.414		118.84	C
ATOM	7423	CE	LYS D	197	−15.895	35.393	−0.433		117.58	C
ATOM	7424	NZ	LYS D	197	−14.589	34.675	−0.468		118.73	N1+
ATOM	7425	H	LYS D	197	−17.383	40.906	−0.373		116.90	H
ATOM	7426	HA	LYS D		197	−19.071	39.146	0.822		117.95	H
ATOM	7427	HB2	LYS D	197	−16.256	39.222	0.913		121.45	H
ATOM	7428	HB3	LYS D	197	−17.075	38.466	2.043		121.45	H
ATOM	7429	HG2	LYS D	197	−17.860	36.941	0.517		120.35	H
ATOM	7430	HG3	LYS D	197	−17.184	37.744	−0.678		120.35	H
ATOM	7431	HD2	LYS D	197	−15.073	37.185	0.128		122.61	H
ATOM	7432	HD3	LYS D	197	−15.738	36.402	1.344		122.61	H
ATOM	7433	HE2	LUS D	197	−16.559	34.792	−0.061		121.10	H
ATOM	7434	HE3	LYS D		197	−16.132	35.630	−1.343		121.10	H
ATOM	7435	HZ1	LYS D	197	−14.658	33.943	−0.969		122.47	H
ATOM	7436	HZ2	LYS D	197	−13.961	35.204	−0.812		122.47	H
ATOM	7437	HZ3	LYS D	197	−14.350	34.440	0.356		122.47	H
ATOM	7438	N	GLY D	198	−19.080	40.155	3.094		120.04	N
ATOM	7439	CA	GLY D	198	−19.195	40.872	4.344		119.36	C
ATOM	7440	C	GLY D	198	−18.810	39.944	5.473		116.53	C
ATOM	7441	O	GLY D	198	−19.383	38.868	5.610		123.62	O
ATOM	7442	H	GLY D	198	−19.482	39.394	3.096		124.05	H
ATOM	7443	HA2	GLY D	198	−18.603	41.640	4.346		123.23	H
ATOM	7444	HA3	GLY D	198	−20.108	41.172	4.476		123.23	H
ATOM	7445	N	TYR D	199	−17.821	40.349	6.262		115.37	N
ATOM	7446	CA	TYR D	199	−17.404	39.590	7.436		116.35	C
ATOM	7447	C	TYR D	199	−17.961	40.233	8.696		119.39	C
ATOM	7448	O	TYR D	199	−17.670	41.391	8.988		122.65	O
ATOM	7449	CB	TYR D	199	−15.879	39.512	7.523		121.01	C
ATOM	7450	CG	TYR D	199	−15.236	38.665	6.450		115.07	C
ATOM	7451	CD1	TYR D	199	−15.126	39.129	5.146		119.90	C
ATOM	7452	CD2	TYR D	199	−14.730	37.408	6.742		117.60	C
ATOM	7453	CE1	TYR D	199	−14.536	38.361	4.162		114.62	C
ATOM	7454	CE2	TYR D	199	−14.134	36.631	5.763		118.84	C
ATOM	7455	CZ	TYR D	199	−14.039	37.115	4.476		115.72	C
ATOM	7456	OH	TYR D	199	−13.448	36.351	3.498		118.51	O
ATOM	7457	H	TYR D	199	−17.370	41.070	6.137		118.44	H
ATOM	7458	HA	TYR D	199	−17.753	38.687	7.375		119.62	H
ATOM	7459	HB2	TYR D	199	−15.517	40.409	7.447		125.22	H
ATOM	7460	HB3	TYR D	199	−15.636	39.133	8.383		125.22	H
ATOM	7461	HD1	TYR D	199	−15.459	39.970	4.930		123.88	H
ATOM	7462	HD2	TYR D	199	−14.792	37.081	7.611		121.12	H
ATOM	7463	HE1	TYR D	199	−14.470	38.685	3.293		117.55	H
ATOM	7464	HE2	TYR D	199	−13.799	35.789	5.973		122.61	H
ATOM	7465	HH	TYR D	199	−13.459	36.762	2.766		122.22	H
ATOM	7466	N	ILE D	200	−18.760	39.478	9.443		124.76	N
ATOM	7467	CA	ILE D	200	−19.354	39.983	10.674		123.61	C
ATOM	7468	C	ILE D	200	−18.272	40.156	11.733		126.05	C
ATOM	7469	O	ILE D	200	−17.486	39.242	11.981		124.51	O
ATOM	7470	CB	ILE D	200	−20.449	39.045	11.204		125.21	C
ATOM	7471	CG1	ILE D	200	−21.472	38.752	10.102		125.80	C
ATOM	7472	CG2	ILE D	200	−21.132	39.664	12.427		127.37	C
ATOM	7473	CD1	ILE D	200	−22.495	37.695	10.470		132.98	C
ATOM	7474	H	ILE D	200	−18.974	38.667	9.257		129.71	H
ATOM	7475	HA	ILE D	200	−19.753	40.850	10.504		128.33	H
ATOM	7476	HB	ILE D	200	−20.037	38.209	11.472		130.25	H
ATOM	7477	HG12	ILE D	200	−21.953	39.569	9.898		130.95	H
ATOM	7478	HG13	ILE D	200	−21.000	38.443	9.313		130.95	H
ATOM	7479	HG21	ILE D	200	−21.818	39.058	12.745		132.84	H
ATOM	7480	HG22	ILE D	200	−20.468	39.807	13.119		132.84	H
ATOM	7481	HG23	ILE D	200	−21.530	40.511	12.170		132.84	H
ATOM	7482	HD11	ILE D	200	−23.102	37.570	9.724		139.58	H
ATOM	7483	HD12	ILE D	200	−22.034	36.864	10.665		139.58	H
ATOM	7484	HD13	ILE D	200	−22.988	37.992	11.251		139.58	H
ATOM	7485	N	GLU D	201	−18.251	41.329	12.359		125.97	N
ATOM	7486	CA	GLU D	201	−17.193	41.698	13.295		127.39	C
ATOM	7487	C	GLU D	201	−17.754	42.496	14.470		126.93	C
ATOM	7488	O	GLU D	201	−18.775	43.171	14.345		125.15	O
ATOM	7489	CB	GLU D	201	−16.114	42.507	12.562		122.39	C
ATOM	7490	CG	GLU D	201	−15.018	43.107	13.435		130.66	C
ATOM	7491	CD	GLU D	201	−14.139	42.058	14.079		134.67	C
ATOM	7492	OE1	GLU D	201	−12.954	41.963	13.696		137.53	O
ATOM	7493	OE2	GLU D	201	−14.628	41.333	14.970		142.28	O1−
ATOM	7494	H	GLU D	201	−18.849	41.939	12.256		131.16	H
ATOM	7495	HA	GLU D	201	−16.782	40.892	13.645		132.87	H
ATOM	7496	HB2	GLU D	201	−15.683	41.926	11.916		126.87	H
ATOM	7497	HB3	GLU D	201	−16.546	43.241	12.097		126.87	H
ATOM	7498	HG2	GLU D	201	−14.454	43.675	12.887		136.80	H
ATOM	7499	HG3	GLU D	201	−15.428	43.629	14.142		136.80	H
ATOM	7500	N	ASN D	202	−17.082	42.406	15.611		131.13	N
ATOM	7501	CA	ASN D	202	−17.415	43.226	16.767		131.58	C
ATOM	7502	C	ASN D	202	−17.351	44.709	16.409		128.02	C
ATOM	7503	O	ASN D	202	−16.326	45.199	15.934		127.55	O
ATOM	7504	CB	ASN D	202	−16.463	42.920	17.926		133.82	C
ATOM	7505	CG	ASN D	202	−16.877	43.595	19.223		140.88	C
ATOM	7506	OD1	ASN D	202	−17.685	44.526	19.228		137.61	O
ATOM	7507	ND2	ASN D	202	−16.317	43.129	20.332		146.74	N
ATOM	7508	H	ASN D	202	−16.421	41.870	15.742		137.35	H
ATOM	7509	HA	ASN D	202	−18.318	43.022	17.055		137.89	H
ATOM	7510	HB2	ASN D	202	−16.449	41.962	18.078		140.59	H
ATOM	7511	HB3	ASN D	202	−15.574	43.232	17.695		140.59	H
ATOM	7512	HD21	ASN D	202	−16.516	43.476	21.094		156.09	H
ATOM	7513	HD22	ASN D	202	−15.754	42.479	20.290		156.09	H
ATOM	7514	N	CYS D	203	−18.448	45.418	16.648		131.67	N
ATOM	7515	CA	CYS D	203	−18.552	46.823	16.270		132.67	C
ATOM	7516	C	CYS D	203	−17.468	47.680	16.919		130.69	C
ATOM	7517	O	CYS D	203	−17.086	48.716	16.382		128.93	O
ATOM	7518	CB	CYS D	203	−19.932	47.370	16.639		128.67	C
ATOM	7519	SG	CYS D	203	−21.284	46.744	15.612		135.00	S
ATOM	7520	H	CYS D	203	−19.152	45.107	17.032		138.00	H
ATOM	7521	HA	CYS D	203	−18.451	46.896	15.308		139.21	H
ATOM	7522	HB2	CYS D	203	−20.125	47.130	17.559		134.41	H
ATOM	7523	HB3	CYS D	203	−19.917	48.336	16.550		134.41	H
ATOM	7524	N	SER D	204	−16.966	47.234	18.066		129.38	N
ATOM	7525	CA	SER D	204	−16.014	48.019	18.843		130.77	C
ATOM	7526	C	SER D	204	−14.590	47.917	18.316		128.07	C
ATOM	7527	O	SER D	204	−13.735	48.720	18.680		128.24	O
ATOM	7528	CB	SER D	204	−16.041	47.577	20.308		133.15	C
ATOM	7529	OG	SER D	204	−17.311	47.822	20.885		137.66	O
ATOM	7530	H	SER D	204	−17.163	46.474	18.418		135.26	H
ATOM	7531	HA	SER D	204	−16.277	48.952	18.809		136.93	H
ATOM	7532	HB2	SER D	204	−15.851	46.627	20.355		139.78	H
ATOM	7533	HB3	SER D	204	−15.370	48.075	20.800		139.78	H
ATOM	7534	HG	SER D	204	−17.314	47.576	21.688		145.19	H
ATOM	7535	N	THR D	205	−14.331	46.924	17.472		131.36	N
ATOM	7536	CA	THR D	205	−12.979	46.684	16.975		130.91	C
ATOM	7537	C	THR D	205	−12.561	47.749	15.956		129.01	C
ATOM	7538	O	THR D	205	−13.268	47.974	14.975		128.55	O
ATOM	7539	CB	THR D	205	−12.869	45.296	16.324		134.84	C
ATOM	7540	OG1	THR D	205	−13.239	44.290	17.277		135.51	O
ATOM	7541	CG2	THR D	205	−11.447	45.032	15.835		130.24	C
ATOM	7542	H	THR D	205	−14.920	46.375	17.171		137.63	H
ATOM	7543	HA	THR D	205	−12.357	46.719	17.719		137.09	H
ATOM	7544	HB	THR D	205	−13.467	45.251	15.562		141.81	H
ATOM	7545	HG1	THR D	205	−13.181	43.529	16.928		142.61	H
ATOM	7546	HG21	THR D	205	−11.394	44.154	15.428		136.29	H
ATOM	7547	HG22	THR D	205	−11.193	45.700	15.179		136.29	H
ATOM	7548	HG23	THR D	205	−10.827	45.072	16.580		136.29	H
ATOM	7549	N	PRO D	206	−11.413	48.410	16.184		124.70	N
ATOM	7550	CA	PRO D	206	−10.936	49.381	15.192		129.16	C
ATOM	7551	C	PRO D	206	−10.597	48.762	13.834		129.75	C
ATOM	7552	O	PRO D	206	−9.898	47.749	13.760		125.31	O
ATOM	7553	CB	PRO D	206	−9.674	49.960	15.845		131.51	C
ATOM	7554	CG	PRO D	206	−9.855	49.738	17.291		128.53	C
ATOM	7555	CD	PRO D	206	−10.598	48.444	17.410		134.12	C
ATOM	7556	HA	PRO D	206	−11.589	50.088	15.070		134.99	H
ATOM	7557	HB2	PRO D	206	−8.892	49.488	15.520		137.81	H
ATOM	7558	HB3	PRO D	206	−9.610	50.908	15.648		137.81	H
ATOM	7559	HG2	PRO D	206	−8.988	49.676	17.721		134.23	H
ATOM	7560	HG3	PRO D	206	−10.372	50.466	17.669		134.23	H
ATOM	7561	HD2	PRO D	206	−9.978	47.698	17.426		140.94	H
ATOM	7562	HD3	PRO D	206	−11.167	48.452	18.195		140.94	H
ATOM	7563	N	ASN D	207	−11.101	49.384	12.772		127.98	N
ATOM	7564	CA	ASN D	207	−10.802	48.982	11.404		125.19	C
ATOM	7565	C	ASN D	207	−10.805	50.193	10.486		122.66	C
ATOM	7566	O	ASN D	207	−11.386	51.228	10.813		122.52	O
ATOM	7567	CB	ASN D	207	−11.816	47.951	10.899		121.57	C
ATOM	7568	CG	ASN D	207	−11.586	46.572	11.476		123.31	C
ATOM	7569	OD1	ASN D	207	−12.271	46.152	12.410		130.03	O
ATOM	7570	ND2	ASN D	207	−10.620	45.858	10.922		121.76	N
ATOM	7571	H	ASN D	207	−11.631	50.060	12.822		133.58	H
ATOM	7572	HA	ASN D	207	−9.919	48.579	11.374		130.23	H
ATOM	7573	HB2	ASN D	207	−12.708	48.237	11.150		125.88	H
ATOM	7574	HB3	ASN D	207	−11.748	47.888	9.933		125.88	H
ATOM	7575	HD21	ASN D	207	−10.448	45.067	11.213		126.11	H
ATOM	7576	HD22	ASN D	207	−10.163	46.185	10.270		126.11	H
ATOM	7577	Z	THR D	208	−10.153	50.066	9.337		121.73	N
ATOM	7578	CA	THR D	208	−10.243	51.086	8.302		117.49	C
ATOM	7579	C	THR D	208	−11.686	51.128	7.807		118.74	C
ATOM	7580	O	THR D	208	−12.457	50.211	8.075		115.97	O
ATOM	7581	CB	THR D	208	−9.287	50.797	7.138		118.70	C
ATOM	7582	OG1	THR D	208	−9.593	49.516	6.576		117.72	O
ATOM	7583	CG2	THR D	208	−7.842	50.802	7.622		123.48	C
ATOM	7584	H	THR D	208	−9.652	49.398	9.132		126.07	H
ATOM	7585	HA	THR D	208	−10.019	51.952	8.678		120.99	H
ATOM	7586	HB	THR D	208	−9.386	51.482	6.458		122.43	H
ATOM	7587	HG1	THR D	208	−9.072	49.351	5.937		121.26	H
ATOM	7588	HG21	THR D	208	−7.244	50.618	6.881		128.17	H
ATOM	7589	HG22	THR D	208	−7.622	51.668	7.999		128.17	H
ATOM	7590	HG23	THR D	208	−7.719	50.121	8.303		128.17	H
ATOM	7591	N	TYR D	209	−12.065	52.188	7.099		118.19	N
ATOM	7592	CA	TYR D	209	−13.438	52.291	6.614		118.43	C
ATOM	7593	C	TYR D	209	−13.528	53.013	5.280		118.76	C
ATOM	7594	O	TYR D	209	−12.606	53.722	4.865		118.98	O
ATOM	7595	CB	TYR D	209	−14.322	52.995	7.651		118.49	C
ATOM	7596	CG	TYR D	209	−13.825	54.355	8.083		119.96	C
ATOM	7597	CD1	TYR D	209	−12.821	54.477	9.032		123.84	C
ATOM	7598	CD2	TYR D	209	−14.367	55.516	7.550		121.18	C
ATOM	7599	CE1	TYR D	209	−12.364	55.717	9.433		123.52	C
ATOM	7600	CE2	TYR D	209	−13.918	56.763	7.947		123.67	C
ATOM	7601	CZ	TYR D	209	−12.914	56.856	8.887		125.34	C
ATOM	7602	OH	TYR D	209	−12.459	58.091	9.288		125.68	O
ATOM	7603	H	TYR D	209	−11.557	52.849	6.888		121.83	H
ATOM	7604	HA	TYR D	209	−13.789	51.396	6.487		122.12	H
ATOM	7605	HB2	TYR D	209	−15.209	53.112	7.275		122.19	H
ATOM	7606	HB3	TYR D	209	−14.375	52.437	8.443		122.19	H
ATOM	7607	HD1	TYR D	209	−12.446	53.711	9.401		128.60	H
ATOM	7608	HD2	TYR D	209	−15.043	55.455	6.914		125.42	H
ATOM	7609	HE1	TYR D	209	−11.688	55.783	10.068		128.22	H
ATOM	7610	HE2	TYR D	209	−14.288	57.533	7.579		128.40	H
ATOM	7611	HH	TYR D	209	−11.853	58.001	9.862		130.82	H
ATOM	7612	N	ILE D	210	−14.657	52.805	4.615		117.13	N
ATOM	7613	CA	ILE D	210	−14.930	53.405	3.322		115.89	C
ATOM	7614	C	ILE D	210	−16.147	54.297	3.433		116.38	C
ATOM	7615	O	ILE D	210	−17.221	53.836	3.825		116.32	O
ATOM	7616	CB	ILE D	210	−15.183	52.337	2.244		115.95	C
ATOM	7617	CG1	ILE D	210	−13.990	51.379	2.155		122.22	C
ATOM	7618	CG2	ILE D	210	−15.457	52.997	0.902		116.76	C
ATOM	7619	CD1	ILE D	210	−14.247	50.150	1.290		122.46	C
ATOM	7620	H	ILE D	210	−15.296	52.307	4.902		120.56	H
ATOM	7621	HA	ILE D	210	−14.173	53.947	3.049		119.06	H
ATOM	7622	HB	ILE D	210	−15.967	51.826	2.498		119.13	H
ATOM	7623	HG12	ILE D	210	−13.235	51.856	1.775		126.67	H
ATOM	7624	HG13	ILE D	210	−13.769	51.072	3.048		126.67	H
ATOM	7625	HG21	ILE D	210	−15.614	52.308	0.238		120.12	H
ATOM	7626	HG22	ILE D	210	−16.240	53.563	0.983		120.12	H
ATOM	7627	HG23	ILE D	210	−14.687	53.531	0.650		120.12	H
ATOM	7628	HD11	ILE D	210	−13.451	49.596	1.284		126.95	H
ATOM	7629	HD12	ILE D	210	−14.993	49.653	1.662		126.95	H
ATOM	7630	HD13	ILE D	210	−14.458	50.438	0.388		126.95	H
ATOM	7631	N	CYS D	211	−15.976	55.568	3.085		114.23	N
ATOM	7632	CA	CYS D	211	−17.094	56.494	3.006		116.85	C
ATOM	7633	C	CYS D	211	−17.596	56.584	1.574		118.03	C
ATOM	7634	O	CYS D	211	−16.827	56.422	0.622		115.29	O
ATOM	7635	CB	CYS D	211	−16.693	57.878	3.515		121.08	C
ATOM	7636	SG	CYS D	211	−16.320	57.907	5.274		127.03	S
ATOM	7637	H	CYS D	211	−15.216	55.919	2.888		117.07	H
ATOM	7638	HA	CYS D	211	−17.819	56.166	3.561		120.22	H
ATOM	7639	HB2	CYS D	211	−15.901	58.171	3.037		125.30	H
ATOM	7640	HB3	CYS D	211	−17.423	58.496	3.354		125.30	H
ATOM	7641	N	MET D	212	−18.892	56.843	1.434		117.13	N
ATOM	7642	CA	MET D	212	−19.522	56.931	0.127		120.63	C
ATOM	7643	C	MET D	212	−20.557	58.047	0.075		121.00	C
ATOM	7644	O	MET D	212	−21.345	58.230	1.007		120.37	O
ATOM	7645	CB	MET D	212	−20.182	55.597	−0.230		118.86	C
ATOM	7646	CG	MET D	212	−21.001	55.619	−1.511		120.28	C
ATOM	7647	SD	MET D	212	−21.817	54.042	−1.811		122.14	S
ATOM	7648	CE	MET D	212	−22.962	54.507	−3.108		127.72	C
ATOM	7649	H	MET D	212	−19.432	56.974	2.090		120.55	H
ATOM	7650	HA	MET D	212	−18.838	57.110	−0.538		124.76	H
ATOM	7651	HB2	MET D	212	−19.488	54.927	−0.336		122.63	H
ATOM	7652	HB3	MET D	212	−20.774	55.341	0.494		122.63	H
ATOM	7653	HG2	MET D	212	−21.684	56.305	−1.441		124.34	H
ATOM	7654	HG3	MET D	212	−20.415	55.805	−2.262		124.34	H
ATOM	7655	HE1	MET D	212	−23.477	53.728	−3.368		133.26	H
ATOM	7656	HE2	MET D	212	−23.554	55.199	−2.773		133.26	H
ATOM	7657	HE3	MET D	212	−22.459	54.841	−3.867		133.26	H
ATOM	7658	N	GLN D	213	−20.540	58.781	−1.031		116.69	N
ATOM	7659	CA	GLN D	213	−21.591	59.731	−1.354		122.03	C
ATOM	7660	C	GLN D	213	−22.309	59.236	−2.599		122.94	C
ATOM	7661	O	GLN D	213	−21.704	59.102	−3.664		120.77	O
ATOM	7662	CB	GLN D	213	−21.026	61.135	−1.587		118.19	C
ATOM	7663	CG	GLN D	213	−20.428	61.794	−0.357		125.42	C
ATOM	7664	CD	GLN D	213	−19.984	63.221	−0.629		127.60	C
ATOM	7665	OE1	GLN D	213	−19.786	63.611	−1.781		128.10	O
ATOM	7666	NE2	GLN D	213	−19.833	64.008	0.431		128.85	N
ATOM	7667	H	GLN D	213	−19.916	58.744	−1.622		120.02	H
ATOM	7668	HA	GLN D	213	−22.229	59.771	−0.624		126.43	H
ATOM	7669	HB2	GLN D	213	−20.328	61.080	−2.258		121.83	H
ATOM	7670	HB3	GLN D	213	−21.741	61.707	−1.908		121.83	H
ATOM	7671	HG2	GLN D	213	−21.095	61.815	0.348		130.50	H
ATOM	7672	HG3	GLN D	213	−19.654	61.287	−0.069		130.50	H
ATOM	7673	HE21	GLN D	213	−19.583	64.825	0.328		134.62	H
ATOM	7674	HE22	GLN D	213	−19.985	63.701	1.220		134.62	H
ATOM	7675	N	ARG D	214	−23.594	58.939	−2.457		125.52	N
ATOM	7676	CA	ARG D	214	−24.407	58.541	−3.592		132.54	C
ATOM	7677	C	ARG D	214	−24.815	59.790	−4.356		140.12	C
ATOM	7678	O	ARG D	214	−25.017	60.850	−3.763		143.97	O
ATOM	7679	CB	ARG D	214	−25.639	57.758	−3.136		130.59	C
ATOM	7680	CG	ARG D	214	−26.467	57.167	−4.271		132.12	C
ATOM	7681	CD	ARG D	214	−25.894	55.846	−4.775		128.20	C
ATOM	7682	NE	ARG D	214	−26.798	55.208	−5.732		127.38	N
ATOM	7683	CZ	ARG D	214	−26.767	55.390	−7.050		128.78	C
ATOM	7684	NH1	ARG D	214	−25.862	56.189	−7.606		127.43	N1+
ATOM	7685	NH2	ARG D	214	−27.649	54.766	−7.819		126.83	N
ATOM	7686	H	ARG D	214	−24.019	58.961	−1.710		130.63	H
ATOM	7687	HA	ARG D	214	−23.885	57.976	−4.183		139.04	H
ATOM	7688	HB2	ARG D	214	−25.349	57.025	−2.571		136.70	H
ATOM	7689	HB3	ARG D	214	−26.215	58.352	−2.630		136.70	H
ATOM	7690	HG2	ARG D	214	−27.369	57.004	−3.954		138.54	H
ATOM	7691	HG3	ARG D	214	−26.481	57.793	−5.012		138.54	H
ATOM	7692	HD2	ARG D	214	−25.047	56.011	−5.220		133.84	H
ATOM	7693	HD3	ARG D	214	−25.768	55.243	−4.026		133.84	H
ATOM	7694	HE	ARG D	214	−27.395	54.674	−5.418		132.85	H
ATOM	7695	HH11	ARG D	214	−25.290	56.599	−7.113		132.91	H
ATOM	7696	HH12	ARG D	214	−25.851	−8.459	56.297		132.91	H
ATOM	7697	HH21	ARG D	214	−28.235	−7.466	54.245		132.19	H
ATOM	7698	HH22	ARG D	214	−27.629	54.875	−8.672		132.19	H
ATOM	7699	N	THR D	215	−24.923	59.656	−5.672		149.40	N
ATOM	7700	CA	THR D	215	−25.345	60.749	−6.538		147.09	C
ATOM	7701	C	THR D	215	−26.665	61.379	−6.091		138.12	C
ATOM	7702	O	THR D	215	−27.251	62.193	−6.808		143.45	O
ATOM	7703	CB	THR D	215	−25.504	60.261	−7.984		143.89	C
ATOM	7704	OG1	THR D	215	−24.958	58.940	−8.113		151.06	O
ATOM	7705	CG2	THR D	215	−24.794	61.194	−8.917		144.94	C
ATOM	7706	H	THR D	215	−24.753	58.927	−6.095		159.28	H
ATOM	7707	HA	THR D	215	−24.664	61.440	−6.528		156.50	H
ATOM	7708	HB	THR D	215	−26.445	60.247	−8.220		152.66	H
ATOM	7709	HG1	THR D	215	−25.043	58.670	−8.903		161.28	H
ATOM	7710	HG21	THR D	215	−25.168	62.086	−8.841		153.93	H
ATOM	7711	HG22	THR D	215	−23.850	61.228	−8.697		153.93	H
ATOM	7712	HG23	THR D	215	−24.893	60.887	−9.832		153.93	H
TER	7713		THR D	215					1
ATOM	7714	N	GLY E	0	−1.565	40.227	−65.921		124.87	N
ATOM	7715	CA	GLY E	0	−1.695	39.502	−64.623		125.57	C
ATOM	7716	C	GLY E	0	−2.109	40.445	−63.512		123.21	C
ATOM	7717	O	GLY E	0	−2.318	41.635	−63.745		121.52	O
ATOM	7718	H1	GLY E	0	−2.226	39.984	−66.465		129.85	H
ATOM	7719	H2	GLY E	0	−1.608	41.105	−65.776		129.85	H
ATOM	7720	H3	GLY E	0	−0.783	40.027	−66.296		129.85	H
ATOM	7721	HA2	GLY E	0	−2.363	38.803	−64.704		130.68	H
ATOM	7722	HA3	GLY E	0	−0.846	39.096	−64.388		130.68	H
ATOM	7723	N	HIS E		1	−2.229	39.916	−62.300		120.53	N
ATOM	7724	CA	HIS E		1	−2.640	40.720	−61.155		119.68	C
ATOM	7725	C	HIS E		1	−1.777	40.422	−59.946		118.24	C
ATOM	7726	O	HIS E		1	−1.189	39.348	−59.847		115.98	O
ATOM	7727	CB	HIS E		1	−4.111	40.469	−60.821		119.17	C
ATOM	7728	CG	HIS E		1	−5.048	40.824	−61.931		122.06	C
ATOM	7729	ND1	HIS E	1	−5.356	42.128	−62.255		123.79	N
ATOM	7730	CD2	HIS E		1	−5.744	40.047	−62.794		122.57	C
ATOM	7731	CE1	HIS E		1	−6.202	42.139	−63.270		122.50	C
ATOM	7732	NE2	HIS E	1	−6.454	40.889	−63.614		122.56	N
ATOM	7733	H	HIS E		1	−2.078	39.090	−62.113		124.63	H
ATOM	7734	HA	HIS E		1	−2.537	41.660	−61.374		123.61	H
ATOM	7735	HB2	HIS E	1	−4.231	39.528	−60.622		123.00	H
ATOM	7736	HB3	HIS E	1	−4.352	41.003	−60.047		123.00	H
ATOM	7737	HD1	HIS E		1	−5.045	42.826	−61.859		128.55	H
ATOM	7738	HD2	HIS E		1	−5.743	39.118	−62.823		127.08	H
ATOM	7739	HE1	HIS E	1	−6.559	42.897	−63.672		127.00	H
ATOM	7740	HE2	HIS E		1	−6.977	40.642	−64.251		127.08	H
ATOM	7741	N	LYS E		2	−1.704	41.383	−59.031		118.21	N
ATOM	7742	CA	LYS E	2	−0.948	41.206	−57.804		117.86	C
ATOM	7743	C	LYS E	2	1.636	41.890	−56.629		119.00	C
ATOM	7744	O	LYS E	2	−2.239	42.957	−56.769		119.28	O
ATOM	7745	CB	LYS E	2	0.478	41.736	−57.970		123.19	C
ATOM	7746	CG	LYS E	2	0.564	43.187	−58.389		127.11	C
ATOM	7747	CD	LYS E	2	1.980	43.554	−58.803		134.68	C
ATOM	7748	CE	LYS E	2	2.079	45.021	−59.188		138.27	C
ATOM	7749	NZ	LYS E	2	3.461	45.403	−59.589		138.97	N1+
ATOM	7750	H	LYS E	2	−2.086	42.150	−59.100		121.85	H
ATOM	7751	HA	LYS E	2	−0.891	40.259	−57.605		121.44	H
ATOM	7752	HB2	LYS E	2	0.943	41.647	−57.123		127.83	H
ATOM	7753	HB3	LYS E	2	0.929	41.208	−58.647		127.83	H
ATOM	7754	HG2	LYS E	2	−0.024	43.338	−59.145		132.53	H
ATOM	7755	HG3	LYS E	2	0.307	43.752	−57.644		132.53	H
ATOM	7756	HD2	LYS E	2	2.584	43.392	−58.061		141.61	H
ATOM	7757	HD3	LYS E	2	2.239	43.020	−59.570		141.61	H
ATOM	7758	HE2	LYS E	2	1.489	45.194	−59.937		145.93	H
ATOM	7759	HE3	LYS E	2	1.824	45.567	−58.428		145.93	H
ATOM	7760	HZ1	LYS E	2	4.024	45.259	−58.915		146.77	H
ATOM	7761	HZ2	LYS E	2	3.719	44.919	−60.290		146.77	H
ATOM	7762	HZ3	LYS E	2	3.487	46.265	−59.808		146.77	H
ATOM	7763	N	LEU E	3	−1.558	41.235	−55.477		115.59	N
ATOM	7764	CA	LEU E	3	−2.079	41.766	−54.229		113.41	C
ATOM	7765	C	LEU E	3	0.905	41.903	−53.273		113.12	C
ATOM	7766	O	LEU E	3	−0.228	40.922	−52.981		112.97	O
ATOM	7767	CB	LEU E	3	−3.160	40.847	−53.661		114.06	C
ATOM	7768	CG	LEU E	3	−3.893	41.275	−52.390		112.36	C
ATOM	7769	CD1	LEU E	3	−4.662	42.573	−52.590		115.83	C
ATOM	7770	CD2	LEU E	3	−4.825	40.167	−51.968		111.74	C
ATOM	7771	H	LEU E	3	−1.197	40.458	−55.394		118.71	H
ATOM	7772	HA	LEU E		3	−2.463	42.644	−54.380		116.10	H
ATOM	7773	HB2	LEU E	3	−3.835	40.727	−54.346		116.87	H
ATOM	7774	HB3	LEU E	3	−2.748	39.990	−53.471		116.87	H
ATOM	7775	HG	LEU E	3	−3.246	41.413	−51.681		114.83	H
ATOM	7776	HD11	LEU E	3	−5.110	42.805	−51.761		118.99	H
ATOM	7777	HD1	LEU E	3	−4.039	43.274	−52.837		118.99	H
ATOM	7778	HD12	LEU E	3	−5.315	42.447	−53.296		118.99	H
ATOM	7779	HD21	LEU E	3	−5.291	40.437	−51.162		114.08	H
ATOM	7780	HD22	LEU E	3	−5.462	40.003	−52.680		114.08	H
ATOM	7781	HD23	LEU E	3	−4.305	39.366	−51.798		114.08	H
ATOM	7782	N	ALA E	4	−0.654	43.124	−52.813		114.08	N
ATOM	7783	CA	ALA E	4	0.497	43.406	−51.961		113.44	C
ATOM	7784	C	ALA E	4	0.060	43.927	−50.597		117.16	C
ATOM	7785	O	ALA E	4	−0.878	44.720	−50.492		116.57	O
ATOM	7786	CB	ALA E	4	1.416	44.405	−52.632		118.34	C
ATOM	7787	H	ALA E	4	−1.140	43.813	−52.981		116.90	H
ATOM	7788	HA	ALA E	4	0.995	42.586	−51.822		116.13	H
ATOM	7789	HB1	ALA E	4	2.172	44.578	−52.050		122.01	H
ATOM	7790	HB2	ALA E	4	1.723	44.035	−53.474		122.01	H
ATOM	7791	HB3	ALA E	4	0.925	45.227	−52.791		122.01	H
ATOM	7792	N	PHE E	5	0.753	43.463	−49.563		115.63	N
ATOM	7793	CA	PHE E	5	0.549	43.919	−48.195		113.64	C
ATOM	7794	C	PHE E	5	1.836	44.553	−47.690		114.46	C
ATOM	7795	O	PHE E	5	2.882	43.911	−47.705		113.48	O
ATOM	7796	CB	PHE E	5	0.153	42.757	−47.285		112.69	C
ATOM	7797	CG	PHE E	5	−1.145	42.107	−47.655		112.18	C
ATOM	7798	CD1	PHE E	5	−1.202	41.174	−48.674		113.36	C
ATOM	7799	CD2	PHE E	5	−2.305	42.415	−46.970		113.02	C
ATOM	7800	CE1	PHE E	5	−2.394	40.571	−49.012		116.36	C
ATOM	7801	CE2	PHE E	5	−3.500	41.813	−47.302		113.36	C
ATOM	7802	CZ	PHE E	5	−3.545	40.890	−48.324		116.42	C
ATOM	7803	H	PHE E	5	1.366	42.864	−49.633		118.75	H
ATOM	7804	HA	PHE E	5	−0.156	44.585	−48.174		116.37	H
ATOM	7805	HB2	PHE E	5	0.845	42.079	−47.327		115.23	H
ATOM	7806	HB3	PHE E	5	0.070	43.087	−46.377		115.23	H
ATOM	7807	HD1	PHE E	5	−0.429	40.956	−49.142		116.03	H
ATOM	7808	HD2	PHE E	5	−2.280	43.038	−46.280		115.63	H
ATOM	7809	HE1	PHE E	5	−2.422	39.947	−49.701		119.63	H
ATOM	7810	HE2	PHE E		5	−4.276	42.030	−46.837		116.03	H
ATOM	7811	HZ	PHE E	5	−4.350	40.483	−48.550		119.70	H
ATOM	7812	N	ASN E	6	1.761	45.806	−47.252		114.65	N
ATOM	7813	CA	ASN E	6	2.928	46.501	−46.714		115.88	C
ATOM	7814	C	ASN E	6	2.745	46.820	−45.232		116.33	C
ATOM	7815	O	ASN E	6	2.007	47.736	−44.871		115.03	O
ATOM	7816	CB	ASN E	6	3.201	47.786	−47.499		119.07	C
ATOM	7817	CG	ASN E	6	4.557	48.391	−47.170		126.15	C
ATOM	7818	OD1	ASN E	6	4.646	49.449	−46.550		133.75	O
ATOM	7819	ND2	ASN E	6	5.622	47.706	−47.572		123.45	N
ATOM	7820	H	ASN E	6	1.042	46.279	−47.255		117.58	H
ATOM	7821	HA	ASN E	6	3.704	45.926	−46.802		119.05	H
ATOM	7822	HB2	ASN E	6	3.181	47.588	−48.448		122.89	H
ATOM	7823	HB3	ASN E	6	2.519	48.441	−47.282		122.89	H
ATOM	7824	HD21	ASN E	6	6.412	48.005	−47.411		128.14	H
ATOM	7825	HD22	ASN E	6	5.522	46.963	−47.994		128.14	H
ATOM	7826	N	PHE E	7	3.411	46.041	−44.385		113.46	N
ATOM	7827	CA	PHE E	7	3.355	46.228	−42.942		116.36	C
ATOM	7828	C	PHE E	7	4.478	47.139	−42.488		115.66	C
ATOM	7829	O	PHE E	7	5.634	46.909	−42.829		114.02	O
ATOM	7830	CB	PHE E	7	3.464	44.888	−42.217		114.45	C
ATOM	7831	CG	PHE E	7	2.371	43.929	−42.549		113.89	C
ATOM	7832	CD1	PHE E	7	2.434	43.159	−43.700		113.75	C
ATOM	7833	CD2	PHE E	7	1.285	43.779	−41.705		113.24	C
ATOM	7834	CE1	PHE E	7	1.425	42.267	−44.007		113.98	C
ATOM	7835	CE2	PHE E	7	0.270	42.887	−42.009		116.30	C
ATOM	7836	CZ	PHE E	7	0.342	42.131	−43.161		116.68	C
ATOM	7837	H	PHE E	7	3.912	45.386	−44.628		116.16	H
ATOM	7838	HA	PHE E	7	2.509	46.639	−42.702		119.63	H
ATOM	7839	HB2	PHE E	7	4.307	44.472	−42.456		117.33	H
ATOM	7840	HB3	PHE E	7	3.437	45.048	−41.260		117.33	H
ATOM	7841	HD1	PHE E	7	3.160	43.248	−44.274		116.50	H
ATOM	7842	HD2	PHE E	7	1.232	44.289	−40.928		115.89	H
ATOM	7843	HE1	PHE E	7	1.474	41.757	−44.784		116.77	H
ATOM	7844	HE2	PHE E	7	−0.457	42.796	−41.437		119.56	H
ATOM	7845	HZ	PHE E	7	−0.337	41.530	−43.367		120.02	H
ATOM	7846	N	ASN E	8	4.139	48.165	−41.715		118.72	N
ATOM	7847	CA	ASN E	8	5.147	49.064	−41.166		117.71	C
ATOM	7848	C	ASN E	8	4.955	49.290	−39.675		118.89	C
ATOM	7849	O	ASN E	8	3.850	49.591	−39.218		116.16	O
ATOM	7850	CB	ASN E	8	5.124	50.406	−41.893		117.97	C
ATOM	7851	CG	ASN E	8	6.231	51.331	−41.433		121.21	C
ATOM	7852	OD1	ASN E	8	7.411	51.033	−41.604		124.65	O
ATOM	7853	ND2	ASN E	8	5.856	52.462	−40.850		123.34	N
ATOM	7854	H	ASN E	8	3.332	48.362	−41.493		122.47	H
ATOM	7855	HA	ASN E	8	6.023	48.669	−41.297		121.25	H
ATOM	7856	HB2	ASN E	8	5.236	50.253	−42.845		121.57	H
ATOM	7857	HB3	ASN E	8	4.275	50.844	−41.724		121.57	H
ATOM	7858	HD21	ASN E	8	6.449	53.019	−40.572		128.01	H
ATOM	7859	HD22	ASN E	8	5.020	52.638	−40.751		128.01	H
ATOM	7860	N	LEU E	9	6.043	49.124	−38.928		115.50	N
ATOM	7861	CA	LEU E	9	6.083	49.460	−37.513		116.76	C
ATOM	7862	C	LEU E	9	7.182	50.492	−37.294		119.62	C
ATOM	7863	O	LEU E	9	8.365	50.183	−37.428		118.29	O
ATOM	7864	CB	LEU E	9	6.330	48.214	−36.656		117.53	C
ATOM	7865	CG	LEU E		9	6.418	48.451	−35.145		116.67	C
ATOM	7866	CD1	LEU E	9	5.120	49.012	−34.599		122.09	C
ATOM	7867	CD2	LEU E	9	6.781	47.164	−34.417		117.22	C
ATOM	7868	H	LEU E	9	6.786	48.811	−39.228		118.60	H
ATOM	7869	HA	LEU E		9	5.236	49.851	−37.249		120.12	H
ATOM	7870	HB2	LEU E	9	5.605	47.589	−36.809		121.03	H
ATOM	7871	HB3	LEU E	9	7.167	47.812	−36.935		121.03	H
ATOM	7872	HG	LEU E	9	7.119	49.099	−34.970		120.00	H
ATOM	7873	HD11	LEU E	9	5.213	49.149	−33.644		126.51	H
ATOM	7874	HD12	LEU E	9	4.933	49.857	−35.038		126.51	H
ATOM	7875	HD13	LEU E	9	4.405	48.381	−34.776		126.51	H
ATOM	7876	HD21	LEU E	9	6.830	47.343	−33.465		120.67	H
ATOM	7877	HD22	LEU E	9	6.098	46.498	−34.594		120.67	H
ATOM	7878	HD23	LEU E	9	7.641	46.851	−34.740		120.67	H
ATOM	7879	N	GLU E	10	6.781	51.720	−36.979		118.79	N
ATOM	7880	CA	GLU E	10	7.726	52.814	−36.766		125.42	C
ATOM	7881	C	GLU E	10	7.809	53.176	−35.290		125.51	C
ATOM	7882	O	GLU E	10	6.822	53.608	−34.700		124.74	O
ATOM	7883	CB	GLU E	10	7.320	54.046	−37.582		123.36	C
ATOM	7884	CG	GLU E	10	8.326	55.197	−37.512		131.78	C
ATOM	7885	CD	GLU E	10	7.883	56.420	−38.300		132.30	C
ATOM	7886	OE1	GLU E	10	6.687	56.775	−38.234		136.09	O
ATOM	7887	OE2	GLU E	10	8.732	57.026	−38.988		136.34	O1−
ATOM	7888	H	GLU E	10	5.958	51.949	−36.880		122.55	H
ATOM	7889	HA	GLU E	10	8.608	52.534	−37.059		130.51	H
ATOM	7890	HB2	GLU E	10	7.230	53.788	−38.512		128.04	H
ATOM	7891	HB3	GLU E	10	6.471	54.375	−37.248		128.04	H
ATOM	7892	HG2	GLU E	10	8.438	55.462	−36.586		138.14	H
ATOM	7893	HG3	GLU E	10	9.174	54.897	−37.876		138.14	H
ATOM	7894	N	ILE E	11	8.988	52.981	−34.703		128.61	N
ATOM	7895	CA	ILE E	11	9.253	53.384	−33.326		125.78	C
ATOM	7896	C	ILE E	11	10.184	54.588	−33.321		124.72	C
ATOM	7897	O	ILE E	11	11.389	54.450	−33.528		124.06	O
ATOM	7898	CB	ILE E	11	9.891	52.248	−32.498		131.17	C
ATOM	7899	CG1	ILE E	11	9.015	50.995	−32.536		130.05	C
ATOM	7900	CG2	ILE E	11	10.114	52.692	−31.056		130.83	C
ATOM	7901	CD1	ILE E	11	9.421	50.004	−33.599		130.44	C
ATOM	7902	H	ILE E	11	9.662	52.612	−35.089		134.34	H
ATOM	7903	HA	ILE E	11	8.420	53.640	−32.900		130.94	H
ATOM	7904	HB	ILE E	11	10.752	52.031	−32.888		137.40	H
ATOM	7905	HG12	ILE E	11	9.070	50.548	−31.677		136.06	H
ATOM	7906	HG13	ILE E	11	8.098	51.259	−32.712		136.06	H
ATOM	7907	HG21	ILE E	11	10.515	51.962	−30.560		137.00	H
ATOM	7908	HG22	ILE E	11	10.706	53.461	−31.051		137.00	H
ATOM	7909	HG23	ILE E	11	9.259	52.930	−30.664		137.00	H
ATOM	7910	HD11	ILE E	11	8.824	49.240	−33.563		136.53	H
ATOM	7911	HD12	ILE E	11	9.361	50.431	−34.468		136.53	H
ATOM	7912	HD13	ILE E	11	10.334	49.719	−33.432		136.53	H
ATOM	7913	N	ASN E	12	9.610	55.765	−33.095		126.17	N
ATOM	7914	CA	ASN E	12	10.364	57.010	−33.023		130.19	C
ATOM	7915	C	ASN E	12	10.274	57.565	−31.611		133.21	C
ATOM	7916	O	ASN E	12	9.309	58.238	−31.259		128.03	O
ATOM	7917	CB	ASN E	12	9.830	58.023	−34.042		128.09	C
ATOM	7918	CG	ASN E	12	10.710	59.256	−34.166		134.34	C
ATOM	7919	OD1	ASN E	12	11.388	59.657	−33.218		128.23	O
ATOM	7920	ND2	ASN E	12	10.701	59.869	−35.347		137.26	N
ATOM	7921	H	ASN E	12	8.765	55.869	−32.977		131.41	H
ATOM	7922	HA	ASN E	12	11.297	56.834	−33.225		136.22	H
ATOM	7923	HB2	ASN E	12	9.784	57.599	−34.914		133.71	H
ATOM	7924	HB3	ASN E	12	8.947	58.312	−33.766		133.71	H
ATOM	7925	HD21	ASN E	12	11.181	60.571	−35.471		144.71	H
ATOM	7926	HD22	ASN E	12	10.214	59.562	−35.986		144.71	H
ATOM	7927	N	GLY E	13	11.280	57.273	−30.797		133.39	N
ATOM	7928	CA	GLY E	13	11.269	57.704	−29.414		137.75	C
ATOM	7929	C	GLY E	13	10.163	57.015	−28.639		137.43	C
ATOM	7930	O	GLY E	13	10.112	55.786	−28.582		137.21	O
ATOM	7931	H	GLY E	13	11.979	56.827	−31.024		140.07	H
ATOM	7932	HA2	GLY E	13	12.120	57.492	−28.998		145.30	H
ATOM	7933	HA3	GLY E	13	11.130	58.663	−29.371		145.30	H
ATOM	7934	N	SER E	14	9.260	57.809	−28.068		144.23	N
ATOM	7935	CA	SER E	14	8.265	57.294	−27.129		148.10	C
ATOM	7936	C	SER E	14	6.947	56.870	−27.780		145.20	C
ATOM	7937	O	SER E	14	6.185	56.108	−27.185		144.70	O
ATOM	7938	CB	SER E	14	7.978	58.343	−26.052		144.32	C
ATOM	7939	OG	SER E	14	7.497	59.546	−26.627		149.63	O
ATOM	7940	H	SER E	14	9.201	58.655	−28.209		153.08	H
ATOM	7941	HA	SER E	14	8.635	56.514	−26.686		157.72	H
ATOM	7942	HB2	SER E	14	7.309	57.995	−25.444		153.18	H
ATOM	7943	HB3	SER E	14	8.799	58.531	−25.570		153.18	H
ATOM	7944	HG	SER E	14	7.345	60.111	−26.024		159.56	H
ATOM	7945	N	ASP E	15	6.670	57.358	−28.986		147.04	N
ATOM	7946	CA	ASP E	15	5.445	56.970	−29.683		151.32	C
ATOM	7947	C	ASP E	15	5.751	55.979	−30.804		146.88	C
ATOM	7948	O	ASP E	15	6.834	55.997	−31.394		142.45	O
ATOM	7949	CB	ASP E	15	4.707	58.201	−30.229		155.08	C
ATOM	7950	CG	ASP E	15	5.515	58.970	−31.250		156.39	C
ATOM	7951	OD1	ASP E	15	6.755	58.979	−31.140		157.41	O
ATOM	7952	OD2	ASP E	15	4.907	59.575	−32.160		164.51	O1−
ATOM	7953	H	ASP E	15	7.168	57.909	−29.420		156.44	H
ATOM	7954	HA	ASP E	15	4.855	56.529	−29.052		161.58	H
ATOM	7955	HB2	ASP E	15	3.884	57.913	−30.654		166.10	H
ATOM	7956	HB3	ASP E	15	4.507	58.801	−29.493		166.10	H
ATOM	7957	N	THR E	16	4.790	55.100	−31.069		140.99	N
ATOM	7958	CA	THR E	16	4.933	54.071	−32.088		135.68	C
ATOM	7959	C	THR E	16	3.735	54.097	−33.026		138.72	C
ATOM	7960	O	THR E	16	2.618	54.422	−32.613		133.45	O
ATOM	7961	CB	THR E	16	5.068	52.671	−31.464		138.05	C
ATOM	7962	OG1	THR E	16	3.910	52.381	−30.674		148.80	O
ATOM	7963	CG2	THR E	16	6.302	52.596	−30.585		139.99	C
ATOM	7964	H	THR E	16	4.032	55.080	−30.662		149.19	H
ATOM	7965	HA	THR E	16	5.731	54.249	−32.611		142.82	H
ATOM	7966	HB	THR E	16	5.153	52.009	−32.168		145.66	H
ATOM	7967	HG1	THR E	16	3.980	51.618	−30.331		158.56	H
ATOM	7968	HG21	THR E	16	6.378	51.711	−30.196		147.99	H
ATOM	7969	HG22	THR E	16	7.095	52.779	−31.112		147.99	H
ATOM	7970	HG23	THR E	16	6.240	53.250	−29.871		147.99	H
ATOM	7971	N	HIS E	17	3.974	53.758	−34.290		131.94	N
ATOM	7972	CA	HIS E	17	2.917	53.737	−35.295		133.04	C
ATOM	7973	C	HIS E	17	2.903	52.408	−36.036		125.75	C
ATOM	7974	O	HIS E	17	3.919	51.976	−36.579		121.85	O
ATOM	7975	CB	HIS E	17	3.093	54.890	−36.284		133.14	C
ATOM	7976	CG	HIS E	17	3.093	56.242	−35.639		143.36	C
ATOM	7977	ND1	HIS E	17	4.224	56.801	−35.083		149.33	N
ATOM	7978	CD2	HIS E	17	2.098	57.141	−35.454		148.56	C
ATOM	7979	CE1	HIS E	17	3.926	57.989	−34.587		147.74	C
ATOM	7980	NE2	HIS E	17	2.643	58.219	−34.799		151.13	N
ATOM	7981	H	HIS E	17	4.747	53.533	−34.592		138.33	H
ATOM	7982	HA	HIS E	17	2.059	53.846	−34.855		139.65	H
ATOM	7983	HB2	HIS E	17	3.940	54.781	−36.744		139.77	H
ATOM	7984	HB3	HIS E	17	2.365	54.867	−36.924		139.77	H
ATOM	7985	HD1	HIS E	17	5.001	56.435	−35.063		159.20	H
ATOM	7986	HD2	HIS E	17	1.213	57.048	−35.722		158.27	H
ATOM	7987	HE1	HIS E	17	4.519	58.565	−34.161		157.28	H
ATOM	7988	HE2	HIS E	17	2.218	58.929	−34.565		161.35	H
ATOM	7989	N	SER E	18	1.744	51.762	−36.039		118.75	N
ATOM	7990	CA	SER E	18	1.548	50.514	−36.761		118.70	C
ATOM	7991	C	SER E	18	0.600	50.766	−37.917		122.66	C
ATOM	7992	O	SER E	18	−0.503	51.269	−37.710		122.11	O
ATOM	7993	CB	SER E	18	0.987	49.434	−35.839		121.15	C
ATOM	7994	OG	SER E	18	1.713	49.382	−34.625		125.66	O
ATOM	7995	H	SER E	18	1.042	52.032	−35.621		122.50	H
ATOM	7996	HA	SER E	18	2.396	50.207	−37.118		122.43	H
ATOM	7997	HB2	SER E	18	0.059	49.637	−35.643		125.38	H
ATOM	7998	HB3	SER E	18	1.052	48.574	−36.283		125.38	H
ATOM	7999	HG	SER E	18	1.396	48.785	−34.125		130.79	H
ATOM	8000	N	THR E	19	1.029	50.431	−39.131		116.84	N
ATOM	8001	CA	THR E	19	0.194	50.639	−40.306		118.45	C
ATOM	8002	C	THR E	19	0.315	49.485	−41.295		115.64	C
ATOM	8003	O	THR E	19	1.355	48.834	−41.386		115.74	O
ATOM	8004	CB	THR E	19	0.553	51.957	−41.024		119.60	C
ATOM	8005	OG1	THR E	19	1.853	51.848	−41.611		127.97	O
ATOM	8006	CG2	THR E	19	0.540	53.128	−40.050		125.33	C
ATOM	8007	H	THR E	19	1.798	50.084	−39.299		120.21	H
ATOM	8008	HA	THR E	19	−0.733	50.696	−40.025		122.14	H
ATOM	8009	HB	THR E	19	−0.100	52.132	−41.720		123.52	H
ATOM	8010	HG1	THR E	19	2.425	51.696	−41.015		133.57	H
ATOM	8011	HG21	THR E	19	0.766	53.948	−40.514		130.39	H
ATOM	8012	HG22	THR E	19	−0.342	53.221	−39.657		130.39	H
ATOM	8013	HG23	THR E	19	1.186	52.977	−39.342		130.39	H
ATOM	8014	N	VAL E	20	−0.767	49.227	−42.020		113.81	N
ATOM	8015	CA	VAL E	20	−0.733	48.293	−43.138		113.33	C
ATOM	8016	C	VAL E	20	−1.448	48.899	−44.341		117.42	C
ATOM	8017	O	VAL E	20	−2.502	49.514	−44.192		115.32	O
ATOM	8018	CB	VAL E	20	−1.387	46.947	−42.794		113.54	C
ATOM	8019	CG1	VAL E	20	−1.103	45.934	−43.893		112.41	C
ATOM	8020	CG2	VAL E	20	−0.887	46.429	−41.450		115.63	C
ATOM	8021	H	VAL E	20	−1.538	49.583	−41.884		116.57	H
ATOM	8022	HA	VAL E	20	0.190	48.127	−43.386		116.00	H
ATOM	8023	HB	VAL E	20	−2.348	47.066	−42.734		116.24	H
ATOM	8024	HG11	VAL E	20	−1.522	45.091	−43.660		114.89	H
ATOM	8025	HG12	VAL E	20	−1.466	46.266	−44.729		114.89	H
ATOM	8026	HG13	VAL E	20	−0.144	45.816	−43.972		114.89	H
ATOM	8027	HG21	VAL E	20	−1.316	45.580	−41.260		118.75	H
ATOM	8028	HG22	VAL E	20	0.075	46.311	−41.496		118.75	H
ATOM	8029	HG23	VAL E	20	−1.109	47.074	−40.761		118.75	H
ATOM	8030	N	ASP E	21	−0.848	48.729	−45.518		115.97	N
ATOM	8031	CA	ASP E	21	−1.440	49.125	−46.794		121.15	C
ATOM	8032	C	ASP E	21	−1.657	47.896	−47.664		118.26	C
ATOM	8033	O	ASP E	21	−0.754	47.072	−47.817		117.18	O
ATOM	8034	CB	ASP E	21	−0.544	50.116	−47.543		122.93	C
ATOM	8035	CG	ASP E	21	−0.289	51.386	−46.761		124.35	C
ATOM	8036	OD1	ASP E	21	−1.220	51.871	−46.088		125.88	O1−
ATOM	8037	OD2	ASP E	21	0.849	51.897	−46.822		127.99	O
ATOM	8038	H	ASP E	21	−0.070	48.373	−45.604		119.17	H
ATOM	8039	HA	ASP E	21	−2.300	49.546	−46.635		125.38	H
ATOM	8040	HB2	ASP E	21	0.312	49.696	−47.720		127.51	H
ATOM	8041	HB3	ASP E	21	−0.973	50.360	−48.378		127.51	H
ATOM	8042	N	VAL E	22	−2.853	47.775	−48.230		115.73	N
ATOM	8043	CA	VAL E	22	−3.147	46.699	−49.170		116.91	C
ATOM	8044	C	VAL E	22	−3.314	47.289	−50.559		118.18	C
ATOM	8045	O	VAL E	22	−4.196	48.120	−50.785		118.14	O
ATOM	8046	CB	VAL E	22	−4.411	45.929	−48.787		113.15	C
ATOM	8047	CG1	VAL E	22	−4.570	44.701	−49.670		118.48	C
ATOM	8048	CG2	VAL E	22	−4.362	45.523	−47.319		114.73	C
ATOM	8049	H	VAL E	22	−3.514	48.305	−48.086		118.88	H
ATOM	8050	HA	VAL E	22	−2.403	46.077	−49.189		120.29	H
ATOM	8051	HB	VAL E	22	−5.184	46.499	−48.919		115.79	H
ATOM	8052	HG11	VAL E	22	−5.376	44.228	−49.411		122.17	H
ATOM	8053	HG12	VAL E	22	−4.635	44.985	−50.595		122.17	H
ATOM	8054	HG13	VAL E	22	−3.797	44.127	−49.554		122.17	H
ATOM	8055	HG21	VAL E	22	−5.172	45.036	−47.099		117.68	H
ATOM	8056	HG22	VAL E	22	−3.587	44.958	−47.173		117.68	H
ATOM	8057	HG23	VAL E	22	−4.298	46.322	−46.773		117.68	H
ATOM	8058	N	ASP E	23	−2.464	46.854	−51.482		115.34	N
ATOM	8059	CA	ASP E	23	−2.482	47.357	−52.849		119.21	C
ATOM	8060	C	ASP E	23	−2.905	46.259	−53.817		119.78	C
ATOM	8061	O	ASP E	23	−2.353	45.158	−53.794		118.41	O
ATOM	8062	CB	ASP E	23	−1.103	47.894	−53.253		121.71	C
ATOM	8063	CG	ASP E	23	−0.614	49.015	−52.347		127.17	C
ATOM	8064	OD1	ASP E	23	−1.453	49.705	−51.735		125.29	O
ATOM	8065	OD2	ASP E	23	0.618	49.212	−52.256		137.02	O1−
ATOM	8066	H	ASP E	23	−1.859	46.260	−51.339		118.40	H
ATOM	8067	HA	ASP E	23	−3.122	48.083	−52.914		123.05	H
ATOM	8068	HB2	ASP E	23	−0.458	47.171	−53.209		126.06	H
ATOM	8069	HB3	ASP E	23	−1.152	48.240	−54.157		126.06	H
ATOM	8070	N	LEU E	24	−3.888	46.567	−54.659		116.92	N
ATOM	8071	CA	LEU E	24	−4.251	45.703	−55.777		117.78	C
ATOM	8072	C	LEU E	24	−3.735	46.318	−57.072		120.26	C
ATOM	8073	O	LEU E	24	−4.165	47.398	−57.462		121.27	O
ATOM	8074	CB	LEU E	24	−5.768	45.506	−55.844		117.65	C
ATOM	8075	CG	LEU E	24	−6.282	44.629	−56.988		120.38	C
ATOM	8076	CD1	LEU E	24	−5.743	43.211	−56.874		120.35	C
ATOM	8077	CD2	LEU E	24	−7.803	44.623	−57.009		121.16	C
ATOM	8078	H	LEU E	24	−4.365	47.280	−54.603		120.30	H
ATOM	8079	HA	LEU E	24	−3.835	44.834	−55.662		121.34	H
ATOM	8080	HB2	LEU E	24	−6.060	45.098	−55.014		121.18	H
ATOM	8081	HB3	LEU E	24	−6.184	46.377	−55.938		121.18	H
ATOM	8082	HG	LEU E	24	−5.973	44.999	−57.831		124.45	H
ATOM	8083	HD11	LEU E	24	−6.087	42.683	−57.612		124.42	H
ATOM	8084	HD12	LEU E	24	−4.774	43.237	−56.909		124.42	H
ATOM	8085	HD13	LEU E	24	−6.034	42.830	−56.031		124.42	H
ATOM	8086	HD21	LEU E	24	−8.106	44.062	−57.740		125.39	H
ATOM	8087	HD22	LEU E	24	−8.128	44.271	−56.165		125.39	H
ATOM	8088	HD23	LEU E	24	−8.120	45.531	−57.134		125.39	H
ATOM	8089	N	ASP E	25	−2.807	45.630	−57.729		119.76	N
ATOM	8090	CA	ASP E	25	−2.193	46.137	−58.953		122.73	C
ATOM	8091	C	ASP E	25	−1.618	47.542	−58.756		127.17	C
ATOM	8092	O	ASP E	25	−1.913	48.462	−59.520		123.98	O
ATOM	8093	CB	ASP E	25	−3.211	46.124	−60.095		121.06	C
ATOM	8094	CG	ASP E	25	−3.666	44.718	−60.449		122.08	C
ATOM	8095	OD1	ASP E	25	−2.862	43.783	−60.271		120.88	O
ATOM	8096	OD2	ASP E	25	−4.820	44.541	−60.895		123.06	O1−
ATOM	8097	H	ASP E	25	−2.513	44.860	−57.485		123.71	H
ATOM	8098	HA	ASP E	25	−1.462	45.550	−59.201		127.28	H
ATOM	8099	HB2	ASP E	25	−3.992	46.636	−59.830		125.27	H
ATOM	8100	HB3	ASP E	25	−2.807	46.518	−60.884		125.27	H
ATOM	8101	N	ASP E	26	−0.796	47.691	−57.720		125.96	N
ATOM	8102	CA	ASP E	26	−0.129	48.958	−57.415		132.50	C
ATOM	8103	C	ASP E	26	−1.125	50.097	−57.208		132.04	C
ATOM	8104	O	ASP E	26	−0.835	51.257	−57.508		130.72	O
ATOM	8105	CB	ASP E	26	0.862	49.324	−58.527		134.94	C
ATOM	8106	CG	ASP E	26	2.007	48.334	−58.635		143.04	C
ATOM	8107	OD1	ASP E	26	2.488	47.863	−57.580		138.49	O
ATOM	8108	OD2	ASP E	26	2.426	48.024	−59.773		145.93	O1−
ATOM	8109	H	ASP E	26	−0.603	47.061	−57.168		131.15	H
ATOM	8110	HA	ASP E	26	0.375	48.854	−56.593		139.00	H
ATOM	8111	HB2	ASP E	26	0.394	49.337	−59.377		141.93	H
ATOM	8112	HB3	ASP E	26	1.237	50.199	−58.341		141.93	H
ATOM	8113	Z	SER E	27	−2.300	49.749	−56.696		127.41	N
ATOM	8114	CA	SER E	27	−3.304	50.730	−56.305		126.12	C
ATOM	8115	C	SER E	27	−3.839	50.370	−54.923		125.00	C
ATOM	8116	O	SER E	27	−4.302	49.252	−54.707		122.30	O
ATOM	8117	CB	SER E	27	−4.438	50.781	−57.328		127.19	C
ATOM	8118	OG	SER E	27	−5.564	51.464	−56.803		135.60	O
ATOM	8119	H	SER E	27	−2.544	48.935	−56.562		132.89	H
ATOM	8120	HA	SER E	27	−2.895	51.608	−56.257		131.34	H
ATOM	8121	HB2	SER E	27	−4.128	51.247	−58.120		132.63	H
ATOM	8122	HB3	SER E	27	−4.697	49.874	−57.556		132.63	H
ATOM	8123	HG	SER E	27	−6.179	51.484	−57.375		142.72	H
ATOM	8124	N	GLN E	28	−3.763	51.311	−53.985		120.78	N
ATOM	8125	CA	GLN E	28	−4.183	51.043	−52.614		121.26	C
ATOM	8126	C	GLN E	28	−5.695	50.879	−52.532		120.87	C
ATOM	8127	O	GLN E	28	−6.443	51.709	−53.055		118.20	O
ATOM	8128	CB	GLN E	28	−3.725	52.167	−51.683		122.63	C
ATOM	8129	CG	GLN E	28	−3.899	51.850	−50.211		123.18	C
ATOM	8130	CD	GLN E	28	−3.629	53.049	−49.326		123.30	C
ATOM	8131	OE1	GLN E	28	−4.462	53.945	−49.208		129.76	O
ATOM	8132	NE2	GLN E	28	−2.458	53.076	−48.708		125.07	N
ATOM	8133	H	GLN E	28	−3.472	52.109	−54.117		124.94	H
ATOM	8134	HA	GLN E	28	−3.774	50.217	−52.313		125.51	H
ATOM	8135	HB2	GLN E	28	−2.784	52.339	−51.840		127.15	H
ATOM	8136	HB3	GLN E	28	−4.242	52.964	−51.878		127.15	H
ATOM	8137	HG2	GLN E	28	−4.812	51.561	−50.054		127.82	H
ATOM	8138	HG3	GLN E	28	−3.279	51.147	−49.962		127.82	H
ATOM	8139	HE21	GLN E	28	−2.257	53.736	−48.194		130.08	H
ATOM	8140	HE22	GLN E	28	−1.897	52.433	−48.820		130.08	H
ATOM	8141	N	ILE E	29	−6.137	49.807	−51.873		116.99	N
ATOM	8142	CA	ILE E	29	−7.560	49.506	−51.751		118.10	C
ATOM	8143	C	ILE E	29	−8.009	49.446	−50.291		117.82	C
ATOM	8144	O	ILE E	29	−9.179	49.671	−49.990		116.96	O
ATOM	8145	CB	ILE E	29	−7.919	48.170	−52.445		117.51	C
ATOM	8146	CG1	ILE E	29	−7.158	46.996	−51.819		118.43	C
ATOM	8147	CG2	ILE E	29	−7.625	48.259	−53.938		121.63	C
ATOM	8148	CD1	ILE E	29	−7.710	45.630	−52.204		114.47	C
ATOM	8149	H	ILE E	29	−5.626	49.235	−51.484		120.39	H
ATOM	8150	HA	ILE E	29	−8.065	50.211	−52.186		121.72	H
ATOM	8151	HB	ILE E	29	−8.869	48.012	−52.331		121.02	H
ATOM	8152	HG12	ILE E	29	−6.233	47.034	−52.108		122.12	H
ATOM	8153	HG13	ILE E	29	−7.204	47.074	−50.853		122.12	H
ATOM	8154	HG21	ILE E	29	−7.855	47.415	−54.356		125.95	H
ATOM	8155	HG22	ILE E	29	−8.155	48.974	−54.322		125.95	H
ATOM	8156	HG23	ILE E	29	−6.681	48.443	−54.063		125.95	H
ATOM	8157	HD11	ILE E	29	−7.179	44.943	−51.771		117.36	H
ATOM	8158	HD12	ILE E	29	−8.632	45.570	−51.911		117.36	H
ATOM	8159	HD13	ILE E	29	−7.660	45.530	−53.167		117.36	H
ATOM	8160	N	ILE E	30	7.077	49.137	−49.395		116.02	N
ATOM	8161	CA	ILE E	30	−7.363	49.058	−47.965		115.82	C
ATOM	8162	0	ILE E	30	−6.210	49.679	−47.184		116.69	C
ATOM	8163	O	ILE E	30	−5.058	49.618	−47.614		118.17	O
ATOM	8164	CB	ILE E	30	−7.569	47.595	−47.501		116.57	C
ATOM	8165	CG1	ILE E	30	−8.733	46.939	−48.247		115.95	C
ATOM	8166	CG2	ILE E	30	−7.827	47.525	−46.004		117.26	C
ATOM	8167	CD1	ILE E	30	−8.751	45.428	−48.111		116.72	C
ATOM	8168	H	ILE E	30	−6.258	48.966	−49.593		119.23	H
ATOM	8169	HA	ILE E	30	−8.170	49.558	−47.769		118.99	H
ATOM	8170	HB	ILE E	30	−6.761	47.096	−47.696		119.88	H
ATOM	8171	HG12	ILE E	30	−9.568	47.280	−47.890		119.14	H
ATOM	8172	HG13	ILE E	30	−8.664	47.153	−49.190		119.14	H
ATOM	8173	HG21	ILE E	30	−7.952	46.598	−45.749		120.72	H
ATOM	8174	HG22	ILE E	30	−7.065	47.899	−45.535		120.72	H
ATOM	8175	HG23	ILE E	30	−8.626	48.036	−45.798		120.72	H
ATOM	8176	HD11	ILE E	30	−9.509	45.076	−48.603		120.06	H
ATOM	8177	HD12	ILE E	30	−7.925	45.069	−48.473		120.06	H
ATOM	8178	HD13	ILE E	30	−8.829	45.196	−47.172		120.06	H
ATOM	8179	N	THR E	31	−6.519	50.278	−46.039		116.82	N
ATOM	8180	CA	THR E	31	−5.482	50.768	−45.141		115.25	C
ATOM	8181	C	THR E	31	−5.893	50.529	−43.693		115.57	C
ATOM	8182	O	THR E	31	−7.079	50.454	−43.371		117.03	O
ATOM	8183	CB	THR E	31	−5.179	52.269	−45.372		120.77	C
ATOM	8184	OG1	THR E	31	−3.995	52.640	−44.653		124.59	O
ATOM	8185	CG2	THR E	31	−6.341	53.143	−44.936		122.38	C
ATOM	8186	H	THR E	31	−7.322	50.414	−45.761		120.18	H
ATOM	8187	HA	THR E	31	−4.665	50.271	−45.304		118.30	H
ATOM	8188	HB	THR E	31	−5.032	52.418	−46.320		124.93	H
ATOM	8189	HG1	THR E	31	−3.342	52.184	−44.919		129.51	H
ATOM	8190	HG21	THR E	31	−6.130	54.077	−45.090		126.85	H
ATOM	8191	HG22	THR E	31	−7.137	52.913	−45.441		126.85	H
ATOM	8192	HG23	THR E	31	−6.518	53.012	−43.991		126.85	H
ATOM	8193	Z	PHE E	32	−4.890	50.416	−42.831		115.94	N
ATOM	8194	CA	PHE E	32	−5.070	50.053	−41.431		116.83	C
ATOM	8195	C	PHE E	32	−4.106	50.905	−40.613		118.16	C
ATOM	8196	O	PHE E	32	−2.923	50.965	−40.937		114.88	O
ATOM	8197	CB	PHE E	32	4.81	48.553	−41.239		112.85	C
ATOM	8198	CG	PHE E	32	−4.831	48.096	−39.805		115.97	C
ATOM	8199	CD1	PHE E	32	−6.027	47.872	−39.151		115.86	C
ATOM	8200	CD2	PHE E	32	−3.646	47.864	−39.121		117.02	C
ATOM	8201	CE1	PHE E	32	−6.045	47.442	−37.834		120.56	C
ATOM	8202	CE2	PHE E	32	−3.658	47.430	−37.807		116.71	C
ATOM	8203	CZ	PHE E	32	−4.858	47.220	−37.163		121.71	C
ATOM	8204	H	PHE E	32	−4.067	50.549	−43.042		119.12	H
ATOM	8205	HA	PHE E	32	−5.978	50.252	−41.154		120.19	H
ATOM	8206	HB2	PHE E	32	−5.494	48.056	−41.716		115.42	H
ATOM	8207	HB3	PHE E	32	−3.937	48.339	−41.603		115.42	H
ATOM	8208	HD1	PHE E	32	−6.829	48.021	−39.597		119.03	H
ATOM	8209	HD2	PHE E	32	−2.834	48.004	−39.551		120.42	H
ATOM	8210	HE1	PHE E	32	−6.857	47.300	−37.402		124.68	H
ATOM	8211	HE2	PHE E	32	−2.856	47.284	−37.358		120.05	H
ATOM	8212	HZ	PHE E	32	−4.868	46.931	−36.279		126.05	H
ATOM	8213	Z	ASP E	33	−4.611	51.580	−39.580		121.77	N
ATOM	8214	CA	ASP E	33	−3.809	52.557	−38.833		124.90	C
ATOM	8215	O	ASP E	33	−3.354	52.053	−37.464		126.03	C
ATOM	8216	O	ASP E	33	2.901	52.838	−36.628		124.42	O
ATOM	8217	CB	ASP E	33	−4.596	53.866	−38.656		123.77	C
ATOM	8218	CG	ASP E	33	−5.878	53.692	−37.849		127.99	C
ATOM	8219	OD1	ASP E	33	−6.013	52.697	−37.102		126.15	O
ATOM	8220	OD2	ASP E	33	−6.762	54.571	−37.959		130.81	O1−
ATOM	8221	H	ASP E	33	−5.415	51.492	−39.290		126.13	H
ATOM	8222	HA	ASP E	33	−3.013	52.761	−39.348		129.88	H
ATOM	8223	HB2	ASP E	33	−4.036	54.509	−38.194		128.52	H
ATOM	8224	HB3	ASP E	33	−4.838	54.207	−39.531		128.52	H
ATOM	8225	N	GLY E	34	−3.480	50.750	−37.238		121.69	N
ATOM	8226	CA	GLY E	34	−3.124	50.158	−35.963		125.18	C
ATOM	8227	C	GLY E	34	−4.353	49.841	−35.137		124.85	C
ATOM	8228	O	GLY E	34	−4.330	48.938	−34.301		124.27	O
ATOM	8229	H	GLY E	34	−3.772	50.184	−37.816		126.03	H
ATOM	8230	HA2	GLY E	34	−2.629	49.338	−36.111		130.22	H
ATOM	8231	HA3	GLY E	34	2.564	50.773	−35.463		130.22	H
ATOM	8232	N	LYS E	35	−5.429	50.583	−35.381		124.67	N
ATOM	8233	CA	LYS E	35	−6.686	50.404	−34.661		127.22	C
ATOM	8234	0	LYS E	35	−7.814	50.034	−35.616		126.78	C
ATOM	8235	O	LYS E	35	−8.439	48.984	−35.477		129.19	O
ATOM	8236	CB	LYS E	35	−7.049	51.681	−33.898		130.19	C
ATOM	8237	CG	LYS E	35	−8.397	51.631	−33.184		133.78	C
ATOM	8238	CD	LYS E	35	−8.744	52.972	−32.557		133.80	C
ATOM	8239	CE	LYS E	35	−10.123	52.940	−31.915		141.60	C
ATOM	8240	NZ	LYS E	35	−10.580	54.294	−31.489		139.39	N1+
ATOM	8241	H	LYS E	35	−5.456	51.209	−35.970		129.61	H
ATOM	8242	HA	LYS E	35	−6.585	49.685	−34.018		132.67	H
ATOM	8243	HB2	LYS E	35	−6.367	51.847	−33.228		136.23	H
ATOM	8244	HB3	LYS E	35	−7.076	52.421	−34.525		136.23	H
ATOM	8245	HG2	LYS E	35	−9.090	51.406	−33.824		140.53	H
ATOM	8246	HG3	LYS E	35	−8.362	50.966	−32.479		140.53	H
ATOM	8247	HD2	LYS E	35	−8.093	53.184	−31.870		140.56	H
ATOM	8248	HD3	LYS E	35	−8.744	53.657	−33.244		140.56	H
ATOM	8249	HE2	LYS E	35	−10.763	52.594	−32.555		149.92	H
ATOM	8250	HE3	LYS E	35	−10.094	52.371	−31.130		149.92	H
ATOM	8251	HZ1	LYS E	35	−10.621	54.837	−32.193		147.26	H
ATOM	8252	HZ2	LYS E	35	−11.387	54.240	−31.118		147.26	H
ATOM	8253	HZ3	LYS E	35	−10.011	54.634	−30.895		147.26	H
ATOM	8254	N	ASP E	36	−8.070	50.912	−36.581		126.84	N
ATOM	8255	CA	ASP E	36	−9.188	50.744	−37.498		125.99	C
ATOM	8256	C	ASP E	36	−8.724	50.409	−38.907		122.89	C
ATOM	8257	O	ASP E	36	−7.639	50.805	−39.332		121.76	O
ATOM	8258	CB	ASP E	36	−10.043	52.011	−37.524		131.28	C
ATOM	8259	CG	ASP E	36	−10.676	52.313	−36.178		134.69	C
ATOM	8260	OD1	ASP E	36	−11.667	51.640	−35.823		135.73	O
ATOM	8261	OD2	ASP E	36	−10.185	53.223	−35.478		137.15	O1−
ATOM	8262	H	ASP E	36	−7.604	51.621	−36.726		132.21	H
ATOM	8263	HA	ASP E	36	−9.744	50.014	−37.185		131.19	H
ATOM	8264	HB2	ASP E	36	−9.485	52.766	−37.769		137.54	H
ATOM	8265	HB3	ASP E	36	−10.756	51.900	−38.173		137.54	H
ATOM	8266	N	ILE E	37	−9.559	49.663	−39.619		120.05	N
ATOM	8267	CA	ILE E	37	−9.321	49.351	−41.018		119.38	C
ATOM	8268	C	ILE E	37	−10.347	50.116	−41.835		118.03	C
ATOM	8269	O	ILE E	37	−11.438	50.406	−41.347		116.80	O
ATOM	8270	CB	ILE E	37	−9.424	47.836	−41.289		117.86	C
ATOM	8271	CG1	ILE E	37	−8.817	47.486	−42.648		117.25	C
ATOM	8272	CG2	ILE E	37	−10.872	47.365	−41.198		120.70	C
ATOM	8273	CD1	ILE E	37	−8.468	46.019	−42.783		117.20	C
ATOM	8274	H	ILE E	37	−10.283	49.319	−39.307		124.06	H
ATOM	8275	HA	ILE E	37	−8.435	49.652	−41.273		123.26	H
ATOM	8276	HB	ILE E	37	8.915	47.374	−40.605		121.43	H
ATOM	8277	HG12	ILE E	37	−9.455	47.707	−43.344		120.70	H
ATOM	8278	HG13	ILE E	37	−8.002	47.999	−42.770		120.70	H
ATOM	8279	HG21	ILE E	37	−10.905	46.411	−41.372		124.84	H
ATOM	8280	HG22	ILE E	37	−11.209	47.550	−40.307		124.84	H
ATOM	8281	HG23	ILE E	37	−11.401	47.841	−41.858		124.84	H
ATOM	8282	HD11	ILE E	37	−8.090	45.864	−43.663		120.64	H
ATOM	8283	HD12	ILE E	37	−7.823	45.784	−42.099		120.64	H
ATOM	8284	HD13	ILE E	37	−9.275	45.492	−42.673		120.64	H
ATOM	8285	N	ARG E	38	−10.007	50.450	−43.072		117.17	N
ATOM	8286	CA	ARG E	38	−10.945	51.180	−43.913		118.63	C
ATOM	8287	C	ARG E	38	−10.678	50.981	−45.400		115.53	C
ATOM	8288	O	ARG E	38	−9.529	50.822	−45.817		113.55	O
ATOM	8289	CB	ARG E	38	−10.905	52.672	−43.576		121.12	C
ATOM	8290	CG	ARG E	38	−9.612	53.367	−43.935		124.59	C
ATOM	8291	CD	ARG E	38	−9.632	54.826	−43.497		134.01	C
ATOM	8292	NE	ARG E	38	−8.473	55.561	−44.000		136.68	N
ATOM	8293	CZ	ARG E	38	−8.437	56.219	−45.156		139.43	C
ATOM	8294	NH1	ARG E	38	−9.501	56.252	−45.953		138.87	N1+
ATOM	8295	NH2	ARG E	38	−7.330	56.851	−45.519		139.19	N
ATOM	8296	H	ARG E	38	−9.253	50.270	−43.444		120.60	H
ATOM	8297	HA	ARG E	38	−11.842	50.859	−43.729		122.36	H
ATOM	8298	HB2	ARG E	38	−11.621	53.117	−44.056		125.34	H
ATOM	8299	HB3	ARG E	38	−11.040	52.777	−42.621		125.34	H
ATOM	8300	HG2	ARG E	38	−8.874	52.925	−43.487		129.50	H
ATOM	8301	HG3	ARG E	38	−9.488	53.339	−44.896		129.50	H
ATOM	8302	HD2	ARG E	38	−10.433	55.252	−43.841		140.81	H
ATOM	8303	HD3	ARG E	38	−9.621	54.869	−42.528		140.81	H
ATOM	8304	HE	ARG E	38	−7.764	55.568	−43.514		144.02	H
ATOM	8305	HH11	ARG E	38	−10.222	55.844	−45.724		146.64	H
ATOM	8306	HH12	ARG E	38	−9.467	56.681	−46.698		146.64	H
ATOM	8307	HH21	ARG E	38	−6.639	56.834	−45.008		147.03	H
ATOM	8308	HH22	ARG E	38	−7.304	57.279	−46.264		147.03	H
ATOM	8309	N	PRO E	39	−11.746	50.991	−46.210		116.34	N
ATOM	8310	CA	PRO E	39	−11.558	50.928	−47.660		117.96	C
ATOM	8311	C	PRO E	39	−11.021	52.249	−48.203		117.79	C
ATOM	8312	O	PRO E	39	−11.322	53.300	−47.639		117.56	O
ATOM	8313	CB	PRO E	39	−12.968	50.636	−48.183		116.77	C
ATOM	8314	CG	PRO E	39	13.872	51.230	−47.161		125.13	C
ATOM	8315	CD	PRO E	39	−13.172	51.069	−45.840		116.34	C
ATOM	8316	HA	PRO E	39	−10.961	50.203	−47.900		121.55	H
ATOM	8317	HB2	PRO E	39	−13.095	51.063	−49.045		120.12	H
ATOM	8318	HB3	PRO E	39	−13.103	49.678	−48.249		120.12	H
ATOM	8319	HG2	PRO E	39	−14.013	52.169	−47.360		130.16	H
ATOM	8320	HG3	PRO E	39	−14.716	50.753	−47.159		130.16	H
ATOM	8321	HD2	PRO E	39	−13.332	51.842	−45.276		119.60	H
ATOM	8322	HD3	PRO E	39	−13.453	50.249	−45.406		119.60	H
ATOM	8323	N	THR E	40	−10.224	52.189	−49.267		116.36	N
ATOM	8324	CA	THR E	40	−9.672	53.389	−49.895		118.13	C
ATOM	8325	C	THR E	40	−9.954	53.377	−51.393		118.97	C
ATOM	8326	O	THR E	40	−9.306	54.076	−52.169		126.46	O
ATOM	8327	CB	THR E	40	−8.149	53.511	−49.662		119.81	C
ATOM	8328	OG1	THR E	40	−7.473	52.405	−50.272		121.82	O
ATOM	8329	CG2	THR E	40	−7.832	53.535	−48.171		120.16	C
ATOM	8330	H	THR E	40	−9.985	51.456	−49.649		119.64	H
ATOM	8331	HA	THR E	40	−10.098	54.172	−49.514		121.76	H
ATOM	8332	HB	THR E	40	−7.829	54.338	−50.055		123.77	H
ATOM	8333	HG1	THR E	40	−7.623	52.397	−51.098		126.18	H
ATOM	8334	HG21	THR E	40	−6.874	53.611	−48.037		124.19	H
ATOM	8335	HG22	THR E	40	−8.270	54.292	−47.752		124.19	H
ATOM	8336	HG23	THR E	40	−8.145	52.718	−47.752		124.19	H
ATOM	8337	N	ILE E	41	−10.930	52.569	−51.783		121.52	N
ATOM	8338	CA	ILE E	41	−11.361	52.471	−53.166		121.60	C
ATOM	8339	C	ILE E	41	−12.865	52.188	−53.133		121.26	C
ATOM	8340	O	ILE E	41	−13.332	51.475	−52.245		120.35	O
ATOM	8341	CB	ILE E	41	−10.587	51.364	−53.925		122.21	C
ATOM	8342	CG1	ILE E	41	−10.776	51.488	−55.437		127.01	C
ATOM	8343	CG2	ILE E	41	−11.002	49.983	−53.443		122.35	C
ATOM	8344	CD1	ILE E	41	−10.107	52.705	−56.037		123.85	C
ATOM	8345	H	ILE E	41	−11.368	52.055	−51.251		125.82	H
ATOM	8346	HA	ILE E	41	−11.214	53.318	−53.616		125.92	H
ATOM	8347	HB	ILE E	41	−9.642	51.476	−53.733		126.65	H
ATOM	8348	HG12	ILE E	41	−10.401	50.702	−55.865		132.41	H
ATOM	8349	HG13	ILE E	41	−11.725	51.546	−55.630		132.41	H
ATOM	8350	HG21	ILE E	41	−10.501	49.313	−53.936		126.82	H
ATOM	8351	HG22	ILE E	41	−10.811	49.908	−52.495		126.82	H
ATOM	8352	HG23	ILE E	41	−11.952	49.867	−53.600		126.82	H
ATOM	8353	HD11	ILE E	41	−10.271	52.716	−56.993		128.62	H
ATOM	8354	HD12	ILE E	41	−10.479	53.503	−55.629		128.62	H
ATOM	8355	HD13	ILE E	41	−9.154	52.659	−55.864		128.62	H
ATOM	8356	N	PRO E	42	−13.636	52.768	−54.072		123.49	N
ATOM	8357	CA	PRO E	42	−15.093	52.589	−54.005		124.92	C
ATOM	8358	C	PRO E	42	−15.578	51.136	−53.948		123.20	C
ATOM	8359	O	PRO E	42	−16.532	50.858	−53.219		122.70	O
ATOM	8360	CB	PRO E	42	−15.575	53.260	−55.294		131.54	C
ATOM	8361	CG	PRO E	42	−14.576	54.332	−55.538		129.15	C
ATOM	8362	CD	PRO E	42	−13.256	53.771	−55.086		124.13	C
ATOM	8363	HA	PRO E	42	−15.451	53.072	−53.245		129.90	H
ATOM	8364	HB2	PRO E	42	−15.577	52.617	−56.020		137.85	H
ATOM	8365	HB3	PRO E	42	−16.460	53.635	−55.159		137.85	H
ATOM	8366	HG2	PRO E	42	−14.551	54.544	−56.484		134.98	H
ATOM	8367	HG3	PRO E	42	−14.809	55.118	−55.019		134.98	H
ATOM	8368	HD2	PRO E	42	−12.799	53.346	−55.828		128.96	H
ATOM	8369	HD3	PRO E	42	−12.713	54.468	−54.685		128.96	H
ATOM	8370	N	PHE E	43	−14.949	50.224	−54.683		122.14	N
ATOM	8371	CA	PHE E	43	−15.479	48.865	−54.768		122.57	C
ATOM	8372	C	PHE E	43	−15.282	48.081	−53.469		119.70	C
ATOM	8373	O	PHE E	43	−15.809	46.981	−53.327		122.95	O
ATOM	8374	CB	PHE E	43	−14.863	48.109	−55.963		122.95	C
ATOM	8375	CG	PHE E	43	−13.453	47.620	−55.747		122.38	C
ATOM	8376	CD1	PHE E	43	−13.203	46.454	−55.040		120.54	C
ATOM	8377	CD2	PHE E	43	−12.382	48.296	−56.303		122.45	C
ATOM	8378	CE1	PHE E	43	−11.912	45.996	−54.859		121.86	C
ATOM	8379	CE2	PHE E	43	−11.085	47.839	−56.127		125.06	C
ATOM	8380	CZ	PHE E	43	−10.852	46.686	−55.403		120.17	C
ATOM	8381	H	PHE E	43	−14.228	50.361	−55.133		126.57	H
ATOM	8382	HA	PHE E	43	−16.434	48.922	−54.926		127.09	H
ATOM	8383	HB2	PHE E	43	−15.415	47.335	−56.156		127.54	H
ATOM	8384	HB3	PHE E	43	−14.854	48.702	−56.731		127.54	H
ATOM	8385	HD1	PHE E	43	−13.913	45.984	−54.667		124.65	H
ATOM	8386	HD2	PHE E	43	−12.532	49.074	−56.789		126.94	H
ATOM	8387	HE1	PHE E	43	−11.759	45.218	−54.372		126.23	H
ATOM	8388	HE2	PHE E	43	−10.372	48.309	−56.496		130.07	H
ATOM	8389	HZ	PHE E	43	−9.983	46.378	−55.283		124.21	H
ATOM	8390	N	MET E	44	−14.556	48.657	−52.513		123.05	N
ATOM	8391	CA	MET E	44	−14.353	48.017	−51.212		121.06	C
ATOM	8392	C	MET E	44	−15.333	48.520	−50.151		122.24	C
ATOM	8393	O	MET E	44	−15.417	47.962	−49.059		119.63	O
ATOM	8394	CB	MET E	44	−12.917	48.239	−50.730		119.76	C
ATOM	8395	CG	MET E	44	−11.878	47.391	−51.456		121.55	C
ATOM	8396	SD	MET E	44	−12.224	45.620	−51.414		121.18	S
ATOM	8397	CE	MET E	44	−12.382	45.323	−49.660		117.95	C
ATOM	8398	H	MET E	44	−14.167	49.420	−52.592		127.65	H
ATOM	8399	HA	MET E	44	−14.480	47.061	−51.318		125.27	H
ATOM	8400	HB2	MET E	44	−12.685	49.171	−50.866		123.72	H
ATOM	8401	HB3	MET E	44	−12.869	48.023	−49.786		123.72	H
ATOM	8402	HG2	MET E	44	−11.846	47.665	−52.386		125.86	H
ATOM	8403	HG3	MET E	44	−11.013	47.534	−51.041		125.86	H
ATOM	8404	HE1	MET E	44	−12.572	44.383	−49.515		121.55	H
ATOM	8405	HE2	MET E	44	−11.550	45.564	−49.223		121.55	H
ATOM	8406	HE3	MET E	44	−13.107	45.865	−49.312		121.55	H
ATOM	8407	N	ILE E	45	−16.073	49.575	−50.467		127.83	N
ATOM	8408	CA	ILE E	45	−17.051	50.108	−49.527		122.95	C
ATOM	8409	C	ILE E	45	−18.164	49.096	−49.288		121.71	C
ATOM	8410	O	ILE E	45	−18.742	48.560	−50.231		121.43	O
ATOM	8411	CB	ILE E	45	−17.634	51.442	−50.029		124.78	C
ATOM	8412	CG1	ILE E	45	−16.560	52.530	−49.916		125.65	C
ATOM	8413	CG2	ILE E	45	−18.877	51.838	−49.221		132.38	C
ATOM	8414	CD1	ILE E	45	−16.940	53.868	−50.511		138.64	C
ATOM	8415	H	ILE E	45	−16.029	49.999	−51.214		133.40	H
ATOM	8416	HA	ILE E	45	−16.612	50.275	−48.678		127.54	H
ATOM	8417	HB	ILE E	45	−17.884	51.344	−50.961		129.73	H
ATOM	8418	HG12	ILE E	45	−16.363	52.672	−48.977		130.78	H
ATOM	8419	HG13	ILE E	45	−15.761	52.223	−50.372		130.78	H
ATOM	8420	HG21	ILE E	45	−19.219	52.680	−49.561		138.86	H
ATOM	8421	HG22	ILE E	45	−19.549	51.145	−49.316		138.86	H
ATOM	8422	HG23	ILE E	45	−18.630	51.934	−48.288		138.86	H
ATOM	8423	HD11	ILE E	45	−16.202	54.487	−50.392		146.36	H
ATOM	8424	HD12	ILE E	45	−17.125	53.752	−51.456		146.36	H
ATOM	8425	HD13	ILE E	45	−17.729	54.203	−50.057		146.36	H
ATOM	8426	N	GLY E	46	−18.445	48.832	−48.015		119.01	N
ATOM	8427	CA	GLY E	46	−19.499	47.909	−47.638		126.57	C
ATOM	8428	C	GLY E	46	−19.056	46.457	−47.589		128.55	C
ATOM	8429	O	GLY E	46	−19.844	45.577	−47.242		127.44	O
ATOM	8430	H	GLY E	46	−18.032	49.181	−47.346		122.81	H
ATOM	8431	HA2	GLY E	46	−19.837	48.152	−46.762		131.88	H
ATOM	8432	HA3	GLY E	46	−20.228	47.981	−48.274		131.88	H
ATOM	8433	N	ASP E	47	−17.800	46.196	−47.936		125.13	N
ATOM	8434	CA	ASP E	47	−17.279	44.834	−47.895		120.13	C
ATOM	8435	C	ASP E	47	−17.364	44.271	−46.477		119.36	C
ATOM	8436	O	ASP E	47	−16.968	44.931	−45.520		123.09	O
ATOM	8437	CB	ASP E	47	−15.838	44.793	−48.394		123.01	C
ATOM	8438	CG	ASP E	47	−15.165	43.465	−48.107		125.88	C
ATOM	8439	OD1	ASP E	47	−15.541	42.456	−48.738		125.43	O
ATOM	8440	OD2	ASP E	47	−14.260	43.431	−47.248		129.08	O1−
ATOM	8441	H	ASP E	47	−17.231	46.786	−48.198		130.15	H
ATOM	8442	HA	ASP E	47	−17.816	44.271	−48.475		124.15	H
ATOM	8443	HB2	ASP E	47	−15.831	44.933	−49.354		127.62	H
ATOM	8444	HB3	ASP E	47	−15.329	45.490	−47.952		127.62	H
ATOM	8445	N	GLU E	48	−17.891	43.056	−46.351		116.14	N
ATOM	8446	CA	GLU E	48	−18.090	42.431	−45.044		121.48	C
ATOM	8447	C	GLU E	48	−17.292	41.133	−44.913		117.74	C
ATOM	8448	O	GLU E	48	−17.473	40.382	−43.958		120.31	O
ATOM	8449	CB	GLU E	48	−19.587	42.164	−44.805		122.20	C
ATOM	8450	CG	GLU E	48	−20.255	41.340	−45.897		125.85	C
ATOM	8451	CD	GLU E	48	−21.750	41.133	−45.672		129.32	C
ATOM	8452	OE1	GLU E	48	−22.447	40.770	−46.643		134.96	O
ATOM	8453	OE2	GLU E	48	−22.226	41.325	−44.535		126.64	O1−
ATOM	8454	H	GLU E	48	−18.143	42.568	−47.012		119.37	H
ATOM	8455	HA	GLU E	48	−17.783	43.040	−44.354		125.77	H
ATOM	8456	HB2	GLU E	48	−19.688	41.684	−43.969		126.64	H
ATOM	8457	HB3	GLU E	48	−20.050	43.015	−44.753		126.64	H
ATOM	8458	HG2	GLU E	48	−20.141	41.793	−46.747		131.02	H
ATOM	8459	HG3	GLU E	48	−19.836	40.466	−45.931		131.02	H
ATOM	8460	N	ILE E	49	−16.399	40.887	−45.867		120.94	N
ATOM	8461	CA	ILE E	49	−15.620	39.649	−45.906		118.17	C
ATOM	8462		ILE E	49	−14.134	39.889	−45.647		117.63	C
ATOM	8463	O	ILE E	49	−13.544	39.294	−44.747		120.44	O
ATOM	8464	CB	ILE E	49	−15.778	38.951	−47.266		121.61	C
ATOM	8465	CG1	ILE E	49	−17.244	38.564	−47.486		123.02	C
ATOM	8466	CG2	ILE E	49	−14.893	37.713	−47.346		120.19	C
ATOM	8467	CD1	ILE E	49	−17.580	38.261	−48.922		130.12	C
ATOM	8468	H	ILE E	49	−16.222	41.428	−46.512		125.13	H
ATOM	8469	HA	ILE E	49	−15.950	39.048	−45.220		121.81	H
ATOM	8470	HB	ILE E	49	−15.512	39.569	−47.965		125.94	H
ATOM	8471	HG12	ILE E	49	−17.442	37.773	−46.961		127.63	H
ATOM	8472	HG13	ILE E	49	−17.808	39.299	−47.198		127.63	H
ATOM	8473	HG21	ILE E	49	−15.014	37.295	−48.213		124.23	H
ATOM	8474	HG22	ILE E	49	−13.967	37.979	−47.233		124.23	H
ATOM	8475	HG23	ILE E	49	−15.149	37.096	−46.643		124.23	H
ATOM	8476	HD11	ILE E	49	−18.519	38.026	−48.983		136.14	H
ATOM	8477	HD12	ILE E	49	−17.400	39.047	−49.461		136.14	H
ATOM	8478	HD13	ILE E	49	−17.033	37.519	−49.224		136.14	H
ATOM	8479	N	PHE E	50	−13.528	40.757	−46.443		114.54	N
ATOM	8480	CA	PHE E	50	−12.085	40.946	−46.383		117.11	C
ATOM	8481	C	PHE E	50	−11.662	41.946	−45.309		116.26	C
ATOM	8482	O	PHE E	50	−10.690	41.706	−44.593		113.97	O
ATOM	8483	CB	PHE E	50	−11.576	41.369	−47.758		115.93	C
ATOM	8484	CG	PHE E	50	−11.833	40.337	−48.816		117.08	C
ATOM	8485	CD1	PHE E	50	−10.955	39.286	−49.001		117.90	C
ATOM	8486	CD2	PHE E	50	−12.980	40.391	−49.591		120.60	C
ATOM	8487	CE1	PHE E	50	−11.200	38.319	−49.958		119.37	C
ATOM	8488	CE2	PHE E	50	−13.230	39.428	−50.552		120.80	C
ATOM	8489	CZ	PHE E	50	−12.342	38.391	−50.733		120.26	C
ATOM	8490	H	PHE E	50	−13.927	41.248	−47.026		117.44	H
ATOM	8491	HA	PHE E		50	−11.672	40.095	−46.167		120.53	H
ATOM	8492	HB2	PHE E	50	−12.024	42.187	−48.023		119.11	H
ATOM	8493	HB3	PHE E	50	−10.618	41.515	−47.709		119.11	H
ATOM	8494	HD1	PHE E	50	−10.186	39.232	−48.480		121.48	H
ATOM	8495	HD2	PHE E	50	−13.584	41.088	−49.472		124.72	H
ATOM	8496	HE1	PHE E	50	−10.598	37.621	−50.081		123.24	H
ATOM	8497	HE2	PHE E		50	−13.999	39.479	−51.073		124.96	H
ATOM	8498	HZ	PHE E	50	−12.507	37.744	−51.381		124.31	H
ATOM	8499	N	LEU E	51	−12.392	43.050	−45.180		116.41	N
ATOM	8500	CA	LEU E	51	−12.055	44.057	−44.177		116.35	C
ATOM	8501	C	LEU E	51	−12.009	43.470	−42.757		115.68	C
ATOM	8502	O	LEU E	51	−11.023	43.665	−42.044		114.16	O
ATOM	8503	CB	LEU E	51	−13.045	45.228	−44.226		117.16	C
ATOM	8504	CG	LEU E	51	−13.007	46.120	−45.473		118.54	C
ATOM	8505	CD1	LEU E	51	−14.064	47.212	−45.365		124.77	C
ATOM	8506	CD2	LEU E	51	−11.630	46.737	−45.699		122.00	C
ATOM	8507	H	LEU E	51	−13.082	43.240	−45.657		119.69	H
ATOM	8508	HA	LEU E	51	−11.174	44.410	−44.377		119.62	H
ATOM	8509	HB2	LEU E	51	−13.943	44.866	−44.161		120.59	H
ATOM	8510	HB3	LEU E	51	−12.875	45.799	−43.461		120.59	H
ATOM	8511	HG	LEU E	51	−13.219	45.579	−46.250		122.25	H
ATOM	8512	HD11	LEU E	51	−14.027	47.767	−46.160		129.72	H
ATOM	8513	HD12	LEU E	51	−14.938	46.799	−45.290		129.72	H
ATOM	8514	HD13	LEU E	51	−13.883	47.749	−44.578		129.72	H
ATOM	8515	HD21	LEU E	51	−11.659	47.289	−46.496		126.40	H
ATOM	8516	HD22	LEU E	51	−11.398	47.278	−44.929		126.40	H
ATOM	8517	HD23	LEU E	51	−10.981	46.025	−45.812		126.40	H
ATOM	8518	N	PRO E	52	−13.065	42.750	−42.337		115.67	N
ATOM	8519	CA	PRO E	52	−13.023	42.226	−40.962		116.66	C
ATOM	8520	C	PRO E	52	−11.952	41.159	−40.777		115.48	C
ATOM	8521	O	PRO E	52	−11.369	41.065	−39.700		115.44	O
ATOM	8522	CB	PRO E	52	−14.425	41.638	−40.758		119.47	C
ATOM	8523	CG	PRO E	52	−14.947	41.399	−42.123		123.22	C
ATOM	8524	CD	PRO E	52	−14.344	42.450	−43.001		119.17	C
ATOM	8525	HA	PRO E	52	−12.878	42.946	−40.328		119.99	H
ATOM	8526	HB2	PRO E	52	−14.362	40.806	−40.264		123.36	H
ATOM	8527	HB3	PRO E	52	−14.982	42.277	−40.285		123.36	H
ATOM	8528	HG2	PRO E	52	−14.680	40.515	−42.421		127.86	H
ATOM	8529	HG3	PRO E	52	−15.914	41.477	−42.117		127.86	H
ATOM	8530	HD2	PRO E	52	−14.189	42.099	−43.892		123.00	H
ATOM	8531	HD3	PRO E	52	−14.908	43.239	−43.021		123.00	H
ATOM	8532	N	PHE E	53	−11.697	40.378	−41.822		113.56	N
ATOM	8533	CA	PHE E	53	−10.656	39.358	−41.790		117.24	C
ATOM	8534	C	PHE E	53	−9.283	40.010	−41.632		114.01	C
ATOM	8535	O	PHE E	53	−8.506	39.630	−40.757		113.44	O
ATOM	8536	CB	PHE E	53	−10.709	38.506	−43.064		116.33	C
ATOM	8537	CG	PHE E	53	−9.659	37.431	−43.128		115.12	C
ATOM	8538	CD1	PHE E	53	−9.837	36.229	−42.465		117.88	C
ATOM	8539	CD2	PHE E	53	−8.505	37.614	−43.867		112.71	C
ATOM	8540	CE1	PHE E	53	−8.878	35.234	−42.530		114.56	C
ATOM	8541	CE2	PHE E	53	−7.540	36.622	−43.934		114.02	C
ATOM	8542	CZ	PHE E	53	−7.729	35.432	−43.263		113.27	C
ATOM	8543	H	PHE E	53	−12.120	40.419	−42.570		116.27	H
ATOM	8544	HA	PHE E	53	−10.804	38.775	−41.030		120.68	H
ATOM	8545	HB2	PHE E	53	−11.577	38.076	−43.115		119.60	H
ATOM	8546	HB3	PHE E	53	−10.585	39.086	−43.832		119.60	H
ATOM	8547	HD1	PHE E	53	−10.611	36.089	−41.967		121.46	H
ATOM	8548	HD2	PHE E	53	−8.372	38.416	−44.320		115.25	H
ATOM	8549	HE1	PHE E	53	−9.008	34.433	−42.076		117.48	H
ATOM	8550	HE2	PHE E	53	−6.766	36.759	−44.431		116.83	H
ATOM	8551	HZ	PHE E	53	−7.083	34.764	−43.307		115.93	H
ATOM	8552	N	TYR E	54	−8.997	41.002	−42.470		112.77	N
ATOM	8553	CA	TYR E	54	−7.711	41.685	−42.426		113.18	C
ATOM	8554	C	TYR E	54	−7.531	42.456	−41.122		114.10	C
ATOM	8555	O	TYR E	54	−6.416	42.550	−40.606		112.95	O
ATOM	8556	CB	TYR E	54	−7.557	42.641	−43.614		113.17	C
ATOM	8557	CG	TYR E	54	−7.431	41.959	−44.968		115.46	C
ATOM	8558	CD1	TYR E	54	−6.845	40.702	−45.094		112.49	C
ATOM	8559	CD2	TYR E	54	−7.897	42.581	−46.121		114.64	C
ATOM	8560	CE1	TYR E	54	−6.735	40.083	−46.336		115.66	C
ATOM	8561	CE2	TYR E	54	−7.789	41.974	−47.361		114.01	C
ATOM	8562	CZ	TYR E	54	−7.212	40.726	−47.462		113.86	C
ATOM	8563	OH	TYR E	54	−7.117	40.130	−48.694		115.59	O
ATOM	8564	H	TYR E	54	−9.532	41.298	−43.074		115.33	H
ATOM	8565	HA	TYR E	54	−7.003	41.024	−42.481		115.81	H
ATOM	8566	HB2	TYR E	54	−8.335	43.219	−43.649		115.80	H
ATOM	8567	HB3	TYR E	54	−6.759	43.176	−43.480		115.80	H
ATOM	8568	HD1	TYR E	54	−6.526	40.267	−44.336		114.99	H
ATOM	8569	HD2	TYR E	54	−8.290	43.421	−46.058		117.56	H
ATOM	8570	HE1	TYR E	54	−6.345	39.241	−46.407		118.79	H
ATOM	8571	HE2	TYR E	54	−8.111	42.403	−48.120		116.81	H
ATOM	8572	HH	TYR E	54	−7.445	40.632	−49.283		118.71	H
ATOM	8573	N	LYS E	55	8.612	43.018	−40.592		111.71	N
ATOM	8574	CA	LYS E	55	−8.514	43.757	−39.335		115.22	C
ATOM	8575	C	LYS E	55	−7.955	42.845	−38.248		113.95	C
ATOM	8576	O	LYS E	55	−7.113	43.257	−37.454		116.50	O
ATOM	8577	CB	LYS E	55	−9.871	44.321	−38.913		116.70	C
ATOM	8578	CG	LYS E	55	9.803	45.205	−37.669		120.44	C
ATOM	8579	CD	LYS E	55	−11.158	45.809	−37.335		127.75	C
ATOM	8580	CE	LYS E	55	−11.074	46.749	−36.141		130.79	C
ATOM	8581	NZ	LYS E	55	−12.385	47.406	−35.858		131.93	N1+
ATOM	8582	H	LYS E	55	−9.401	42.989	−40.931		114.05	H
ATOM	8583	HA	LYS E	55	−7.902	44.500	−39.451		118.27	H
ATOM	8584	HB2	LYS E	55	−10.227	44.857	−39.639		120.04	H
ATOM	8585	HB3	LYS E	55	−10.471	43.584	−38.722		120.04	H
ATOM	8586	HG2	LYS E	55	−9.515	44.671	−36.912		124.53	H
ATOM	8587	HG3	LYS E	55	−9.178	45.930	−37.825		124.53	H
ATOM	8588	HD2	LYS E	55	−11.479	46.315	−38.098		133.29	H
ATOM	8589	HD3	LYS E	55	−11.780	45.098	−37.118		133.29	H
ATOM	8590	HE2	LYS E	55	−10.812	46.244	−35.355		136.95	H
ATOM	8591	HE3	LYS E	55	−10.421	47.443	−36.326		136.95	H
ATOM	8592	HZ1	LYS E	55	−12.308	47.949	−35.157		138.32	H
ATOM	8593	HZ2	LYS E	55	−12.645	47.881	−36.565		138.32	H
ATOM	8594	HZ3	LYS E	55	−13.001	46.790	−35.681		138.32	H
ATOM	8595	N	ASN E	56	−8.406	41.596	−38.236		112.27	N
ATOM	8596	CA	ASN E	56	7.924	40.627	−37.264		113.08	C
ATOM	8597	C	ASN E	56	−6.491	40.185	−37.546		115.68	C
ATOM	8598	O	ASN E	56	−5.659	40.159	−36.642		113.45	O
ATOM	8599	CB	ASN E	56	−8.843	39.404	−37.234		120.81	C
ATOM	8600	CG	ASN E	56	−10.166	39.686	−36.549		125.65	C
ATOM	8601	OD1	ASN E	56	−10.228	40.453	−35.587		132.51	O
ATOM	8602	ND2	ASN E	56	−11.234	39.066	−37.040		127.48	N
ATOM	8603	H	ASN E	56	−8.993	41.285	−38.782		114.72	H
ATOM	8604	HA	ASN E	56	−7.941	41.032	−36.383		115.70	H
ATOM	8605	HB2	ASN E	56	−9.029	39.126	−38.145		124.97	H
ATOM	8606	HB3	ASN E	56	−8.402	38.687	−36.752		124.97	H
ATOM	8607	HD21	ASN E	56	−12.007	39.194	−36.685		132.98	H
ATOM	8608	HD22	ASN E	56	−11.152	38.536	−37.712		132.98	H
ATOM	8609	N	VAL E	57	−6.209	39.830	−38.795		112.98	N
ATOM	8610	CA	VAL E	57	−4.869	39.403	−39.172		111.78	C
ATOM	8611	0	VAL E	57	−3.849	40.512	−38.932		110.70	C
ATOM	8612	O	VAL E	57	−2.742	40.250	−38.470		112.79	O
ATOM	8613	CB	VAL E	57	−4.811	38.970	−40.651		115.00	C
ATOM	8614	CG1	VAL E	57	−3.373	38.701	−41.085		113.02	C
ATOM	8615	CG2	VAL E	57	−5.665	37.734	−40.867		111.75	C
ATOM	8616	H	VAL E	57	−6.776	39.828	−39.441		115.57	H
ATOM	8617	HA	VAL E	57	−4.616	38.641	−38.627		114.14	H
ATOM	8618	HB	VAL E	57	−5.166	39.682	−41.205		118.00	H
ATOM	8619	HG11	VAL E	57	−3.369	38.432	−42.016		115.62	H
ATOM	8620	HG12	VAL E	57	−2.853	39.513	−40.972		115.62	H
ATOM	8621	HG13	VAL E	57	−3.004	37.993	−40.533		115.62	H
ATOM	8622	HG21	VAL E	57	−5.617	37.476	−41.801		114.10	H
ATOM	8623	HG22	VAL E	57	−5.327	37.016	−40.308		114.10	H
ATOM	8624	HG23	VAL E	57	−6.582	37.938	−40.626		114.10	H
ATOM	8625	N	PHE E	58	−4.216	41.746	−39.259		112.71	N
ATOM	8626	CA	PHE E	58	−3.288	42.862	−39.119		112.91	C
ATOM	8627	C	PHE E	58	−3.030	43.177	−37.645		115.14	C
ATOM	8628	O	PHE E	58	−1.881	43.346	−37.236		112.36	O
ATOM	8629	CB	PHE E	58	−3.814	44.103	−39.851		110.07	C
ATOM	8630	CG	PHE E	58	−3.890	43.946	−41.352		113.18	C
ATOM	8631	CD1	PHE E	58	−3.394	42.810	−41.982		113.27	C
ATOM	8632	CD2	PHE E	58	−4.463	44.938	−42.135		115.09	C
ATOM	8633	CE1	PHE E	58	−3.470	42.667	−43.360		114.15	C
ATOM	8634	CE2	PHE E	58	−4.542	44.799	−43.518		114.94	C
ATOM	8635	CZ	PHE E	58	−4.045	43.664	−44.127		115.54	C
ATOM	8636	H	PHE E	58	−4.991	41.964	−39.561		115.25	H
ATOM	8637	HA	PHE E	58	−2.441	42.616	−39.523		115.49	H
ATOM	8638	HB2	PHE E	58	−4.708	44.300	−39.529		112.09	H
ATOM	8639	HB3	PHE E	58	−3.226	44.850	−39.662		112.09	H
ATOM	8640	HD1	PHE E	58	−3.008	42.135	−41.471		115.93	H
ATOM	8641	HD2	PHE E	58	−4.801	45.703	−41.731		118.11	H
ATOM	8642	HE1	PHE E	58	−3.134	41.902	−43.768		116.98	H
ATOM	8643	HE2	PHE E	58	−4.928	45.471	−44.032		117.92	H
ATOM	8644	HZ	PHE E	58	−4.095	43.571	−45.051		118.65	H
ATOM	8645	N	SER E	59	−4.088	43.250	−36.844		112.44	N
ATOM	8646	CA	SER E	59	−3.935	43.540	−35.418		115.47	C
ATOM	8647	C	SER E	59	−3.058	42.488	−34.743		115.91	C
ATOM	8648	O	SER E	59	−2.148	42.820	−33.978		114.84	O
ATOM	8649	CB	SER E	59	−5.299	43.608	−34.727		119.05	C
ATOM	8650	OG	SER E	59	−6.086	44.656	−35.260		126.66	O
ATOM	8651	H	SER E	59	−4.902	43.137	−37.098		114.93	H
ATOM	8652	HA	SER E	59	−3.503	44.402	−35.315		118.56	H
ATOM	8653	HB2	SER E	59	−5.763	42.766	−34.860		122.86	H
ATOM	8654	HB3	SER E	59	−5.165	43.766	−33.779		122.86	H
ATOM	8655	HG	SER E	59	−6.211	44.532	−36.082		131.99	H
ATOM	8656	N	GLU E	60	−3.325	41.221	−35.046		114.24	N
ATOM	8657	CA	GLU E	60	−2.553	40.120	−34.483		116.08	C
ATOM	8658	C	GLU E	60	−1.097	40.145	−34.956		114.22	C
ATOM	8659	O	GLU E	60	−0.192	39.806	−34.197		118.48	O
ATOM	8660	CB	GLU E	60	−3.198	38.780	−34.844		119.87	C
ATOM	8661	CG	GLU E	60	−4.571	38.559	−34.219		127.96	C
ATOM	8662	CD	GLU E	60	−4.514	38.305	−32.722		141.64	C
ATOM	8663	OE1	GLU E	60	−3.399	38.165	−32.175		141.26	O
ATOM	8664	OE2	GLU E	60	−5.592	38.243	−32.090		150.70	O1−
ATOM	8665	H	GLU E	60	−3.952	40.972	−35.579		117.09	H
ATOM	8666	HA	GLU E	60	−2.553	40.199	−33.517		119.30	H
ATOM	8667	HB2	GLU E	60	−3.302	38.734	−35.808		123.84	H
ATOM	8668	HB3	GLU E	60	−2.618	38.064	−34.543		123.84	H
ATOM	8669	HG2	GLU E	60	−5.114	39.348	−34.367		133.56	H
ATOM	8670	HG3	GLU E	60	−4.986	37.788	−34.637		133.56	H
ATOM	8671	Z	PHE E	61	−0.873	40.545	−36.206		115.60	N
ATOM	8672	CA	PHE E	61	0.484	40.651	−36.745		114.83	C
ATOM	8673	C	PHE E	61	1.364	41.506	−35.841		113.77	C
ATOM	8674	O	PHE E	61	2.510	41.154	−35.556		115.86	O
ATOM	8675	CB	PHE E	61	0.466	41.242	−38.161		113.27	C
ATOM	8676	CG	PHE E	61	1.838	41.467	−38.745		110.38	C
ATOM	8677	CD1	PHE E	61	2.456	40.482	−39.495		110.57	C
ATOM	8678	CD2	PHE E	61	2.506	42.668	−38.548		112.22	C
ATOM	8679	CE1	PHE E	61	3.722	40.689	−40.033		113.44	C
ATOM	8680	CE2	PHE E	61	3.764	42.881	−39.087		112.04	C
ATOM	8681	CZ	PHE E	61	4.372	41.889	−39.825		112.36	C
ATOM	8682	H	PHE E	61	−1.491	40.762	−36.764		118.72	H
ATOM	8683	HA	PHE E	61	0.875	39.764	−36.795		117.79	H
ATOM	8684	HB2	PHE E	61	0.010	40.634	−38.748		115.92	H
ATOM	8685	HB3	PHE E	61	0.011	42.099	−38.136		115.92	H
ATOM	8686	HD1	PHE E	61	2.022	39.671	−39.635		112.69	H
ATOM	8687	HD2	PHE E	61	2.102	43.341	−38.049		114.66	H
ATOM	8688	HE1	PHE E	61	4.129	40.019	−40.534		116.13	H
ATOM	8689	HE2	PHE E	61	4.201	43.689	−38.944		114.45	H
ATOM	8690	HZ	PHE E	61	5.217	42.029	−40.187		114.83	H
ATOM	8691	N	PHE E	62	0.821	42.630	−35.385		113.88	N
ATOM	8692	CA	PHE E	62	1.579	43.544	−34.541		115.96	C
ATOM	8693	C	PHE E	62	1.603	43.105	−33.079		114.71	C
ATOM	8694	O	PHE E	62	2.630	43.211	−32.414		111.05	O
ATOM	8695	CB	PHE E	62	1.008	44.956	−34.649		116.31	C
ATOM	8696	CG	PHE E	62	1.245	45.598	−35.986		116.94	C
ATOM	8697	CD1	PHE E	62	2.509	46.039	−36.340		116.08	C
ATOM	8698	CD2	PHE E	62	0.207	45.758	−36.888		113.45	C
ATOM	8699	CE1	PHE E	62	2.734	46.631	−37.569		116.16	C
ATOM	8700	CE2	PHE E	62	0.424	46.349	−38.117		115.64	C
ATOM	8701	CZ	PHE E	62	1.691	46.784	−38.459		117.68	C
ATOM	8702	H	PHE E	62	0.017	42.886	−35.551		116.66	H
ATOM	8703	HA	PHE E	62	2.496	43.571	−34.856		119.16	H
ATOM	8704	HB2	PHE E	62	0.049	44.918	−34.503		119.58	H
ATOM	8705	HB3	PHE E	62	1.422	45.515	−33.973		119.58	H
ATOM	8706	HD1	PHE E	62	3.214	45.937	−35.743		119.30	H
ATOM	8707	HD2	PHE E	62	−0.647	45.467	−36.663		116.15	H
ATOM	8708	HE1	PHE E	62	3.587	46.923	−37.795		119.39	H
ATOM	8709	HE2	PHE E	62	−0.281	46.451	−38.715		118.77	H
ATOM	8710	HZ	PHE E	62	1.839	47.182	−39.287		121.21	H
ATOM	8711	N	SER E	63	0.479	42.603	−32.580		114.62	N
ATOM	8712	CA	SER E	63	0.375	42.269	−31.163		117.58	C
ATOM	8713	C	SER E	63	1.149	40.993	−30.833		118.25	C
ATOM	8714	O	SER E	63	1.469	40.744	−29.675		115.30	O
ATOM	8715	CB	SER E	63	−1.092	42.124	−30.749		121.93	C
ATOM	8716	OG	SER E	63	−1.698	41.011	−31.375		126.07	O
ATOM	8717	H	SER E	63	−0.233	42.446	−33.036		117.54	H
ATOM	8718	HA	SER E	63	0.760	42.992	−30.643		121.09	H
ATOM	8719	HB2	SER E	63	−1.136	42.007	−29.787		126.31	H
ATOM	8720	HB3	SER E	63	−1.571	42.928	−31.006		126.31	H
ATOM	8721	HG	SER E	63	−2.501	40.948	−31.136		131.29	H
ATOM	8722	N	LEU E	64	1.453	40.196	−31.854		115.25	N
ATOM	8723	CA	LEU E	64	2.259	38.989	−31.684		116.15	C
ATOM	8724	C	LEU E	64	3.760	39.284	−31.762		118.76	C
ATOM	8725	O	LEU E	64	4.583	38.437	−31.411		113.28	O
ATOM	8726	CB	LEU E	64	1.895	37.948	−32.745		118.37	C
ATOM	8727	CG	LEU E	64	0.535	37.263	−32.613		126.98	C
ATOM	8728	CD1	LEU E	64	0.210	36.496	−33.888		124.22	C
ATOM	8729	CD2	LEU E	64	0.517	36.335	−31.413		122.89	C
ATOM	8730	H	LEU E	64	1.201	40.334	−32.665		118.30	H
ATOM	8731	HA	LEU E	64	2.074	38.606	−30.813		119.38	H
ATOM	8732	HB2	LEU E	64	1.912	38.384	−33.612		122.05	H
ATOM	8733	HB3	LEU E	64	2.569	37.251	−32.725		122.05	H
ATOM	8734	HG	LEU E	64	−0.150	37.938	−32.483		132.37	H
ATOM	8735	HD11	LEU E	64	−0.655	36.069	−33.787		129.07	H
ATOM	8736	HD12	LEU E	64	0.187	37.118	−34.633		129.07	H
ATOM	8737	HD13	LEU E	64	0.895	35.827	−34.037		129.07	H
ATOM	8738	HD21	LEU E	64	−0.355	35.915	−31.353		127.46	H
ATOM	8739	HD22	LEU E	64	1.203	35.660	−31.526		127.46	H
ATOM	8740	HD23	LEU E	64	0.691	36.853	−30.611		127.46	H
ATOM	8741	N	PHE E	65	4.118	40.475	−32.233		116.54	N
ATOM	8742	CA	PHE E	65	5.526	40.845	−32.337		116.39	C
ATOM	8743	C	PHE E	65	6.045	41.265	−30.970		118.01	C
ATOM	8744	O	PHE E	65	5.574	42.242	−30.391		117.22	O
ATOM	8745	CB	PHE E	65	5.726	41.971	−33.354		114.80	C
ATOM	8746	CG	PHE E	65	7.166	42.375	−33.535		114.42	C
ATOM	8747	CD1	PHE E	65	8.128	41.434	−33.870		116.17	C
ATOM	8748	CD2	PHE E	65	7.554	43.693	−33.380		115.24	C
ATOM	8749	CE1	PHE E	65	9.454	41.805	−34.040		114.97	C
ATOM	8750	CE2	PHE E	65	8.876	44.070	−33.549		114.62	C
ATOM	8751	CZ	PHE E	65	9.824	43.127	−33.876		116.09	C
ATOM	8752	H	PHE E	65	3.569	41.082	−32.497		119.85	H
ATOM	8753	HA	PHE E	65	6.038	40.075	−32.632		119.67	H
ATOM	8754	HB2	PHE E	65	5.390	41.678	−34.216		117.76	H
ATOM	8755	HB3	PHE E	65	5.234	42.752	−33.057		117.76	H
ATOM	8756	HD1	PHE E	65	7.883	40.544	−33.979		119.41	H
ATOM	8757	HD2	PHE E	65	6.919	44.335	−33.157		118.29	H
ATOM	8758	HE1	PHE E	65	10.092	41.166	−34.262		117.96	H
ATOM	8759	HE2	PHE E	65	9.124	44.959	−33.439		117.55	H
ATOM	8760	HZ	PHE E	65	10.712	43.379	−33.991		119.31	H
ATOM	8761	N	ARG E	66	7.018	40.520	−30.459		118.88	N
ATOM	8762	CA	ARG E	66	7.536	40.756	−29.118		120.69	C
ATOM	8763	C	ARG E	66	8.694	41.748	−29.143		118.93	C
ATOM	8764	O	ARG E	66	9.834	41.401	−28.836		116.41	O
ATOM	8765	CB	ARG E	66	7.968	39.434	−28.484		125.21	C
ATOM	8766	CG	ARG E	66	6.879	38.373	−28.539		129.70	C
ATOM	8767	CD	ARG E	66	7.008	37.358	−27.421		135.51	C
ATOM	8768	NE	ARG E	66	8.129	36.441	−27.606		145.62	N
ATOM	8769	CZ	ARG E	66	8.038	35.247	−28.185		149.30	C
ATOM	8770	NH1	ARG E	66	6.876	34.804	−28.652		148.42	N1+
ATOM	8771	NH2	ARG E	66	9.117	34.488	−28.298		150.83	N
ATOM	8772	H	ARG E	66	7.397	39.868	−30.872		122.66	H
ATOM	8773	HA	ARG E	66	6.831	41.134	−28.570		124.83	H
ATOM	8774	HB2	ARG E	66	8.743	39.094	−28.958		130.25	H
ATOM	8775	HB3	ARG E	66	8.190	39.588	−27.552		130.25	H
ATOM	8776	HG2	ARG E	66	6.013	38.803	−28.458		135.64	H
ATOM	8777	HG3	ARG E	66	6.939	37.901	−29.384		135.64	H
ATOM	8778	HD2	ARG E	66	7.142	37.828	−26.583		142.61	H
ATOM	8779	HD3	ARG E	66	6.195	36.831	−27.378		142.61	H
ATOM	8780	HE	ARG E	66	8.901	36.691	−27.322		154.74	H
ATOM	8781	HH11	ARG E	66	6.170	35.290	−28.581		158.11	H
ATOM	8782	HH12	ARG E	66	6.829	34.030	−29.025		158.11	H
ATOM	8783	HH21	ARG E	66	9.873	34.768	−27.999		160.99	H
ATOM	8784	HH22	ARG E	66	9.062	33.716	−28.674		160.99	H
ATOM	8785	N	ARG E	67	8.380	42.984	−29.513		118.67	N
ATOM	8786	CA	ARG E	67	9.361	44.059	−29.578		120.20	C
ATOM	8787	C	ARG E	67	10.020	44.281	−28.218		121.69	C
ATOM	8788	O	ARG E	67	9.332	44.366	−27.204		117.08	O
ATOM	8789	CB	ARG E	67	8.685	45.349	−30.057		121.97	C
ATOM	8790	CG	ARG E	67	9.601	46.559	−30.135		127.90	C
ATOM	8791	CD	ARG E	67	8.884	47.772	−30.720		140.95	C
ATOM	8792	NE	ARG E	67	8.218	48.579	−29.698		159.70	N
ATOM	8793	CZ	ARG E	67	6.960	48.412	−29.296		172.67	C
ATOM	8794	NH1	ARG E	67	6.199	47.460	−29.821		175.12	N1+
ATOM	8795	NH2	ARG E	67	6.457	49.206	−28.360		172.00	N
ATOM	8796	H	ARG E	67	7.587	43.230	−29.736		122.41	H
ATOM	8797	HA	ARG E	67	10.053	43.823	−30.216		124.24	H
ATOM	8798	HB2	ARG E	67	8.323	45.197	−30.944		126.37	H
ATOM	8799	HB3	ARG E	67	7.964	45.566	−29.444		126.37	H
ATOM	8800	HG2	ARG E	67	9.906	46.787	−29.243		133.48	H
ATOM	8801	HG3	ARG E	67	10.358	46.350	−30.705		133.48	H
ATOM	8802	HD2	ARG E	67	9.532	48.335	−31.172		149.14	H
ATOM	8803	HD3	ARG E	67	8.211	47.468	−31.349		149.14	H
ATOM	8804	HE	ARG E	67	8.673	49.208	−29.328		171.64	H
ATOM	8805	HH11	ARG E	67	6.518	46.941	−30.429		190.15	H
ATOM	8806	HH12	ARG E	67	5.388	47.361	−29.554		190.15	H
ATOM	8807	HH21	ARG E	67	6.944	49.825	−28.014		186.40	H
ATOM	8808	HH22	ARG E	67	5.645	49.101	−28.097		186.40	H
ATOM	8809	N	VAL E	68	11.348	44.362	−28.193		122.03	N
ATOM	8810	CA	VAL E	68	12.059	44.659	−26.953		120.34	C
ATOM	8811	C	VAL E	68	12.343	46.156	−26.894		122.74	C
ATOM	8812	Q	VAL E	68	12.682	46.762	−27.912		125.42	Q
ATOM	8813	CB	VAL E	68	13.384	43.867	−26.823		127.96	C
ATOM	8814	CG1	VAL E	68	13.108	42.374	−26.817		130.54	C
ATOM	8815	CG2	VAL E	68	14.361	44.220	−27.936		128.18	C
ATOM	8816	H	VAL E	68	11.858	44.250	−28.877		126.44	H
ATOM	8817	HA	VAL E	68	11.494	44.428	−26.199		124.41	H
ATOM	8818	HB	VAL E	68	13.803	44.095	−25.978		133.55	H
ATOM	8819	HG11	VAL E	68	13.950	41.899	−26.735		136.65	H
ATOM	8820	HG12	VAL E	68	12.534	42.163	−26.064		136.65	H
ATOM	8821	HG13	VAL E	68	12.670	42.131	−27.647		136.65	H
ATOM	8822	HG21	VAL E	68	15.174	43.705	−27.818		133.82	H
ATOM	8823	HG22	VAL E	68	13.954	44.008	−28.791		133.82	H
ATOM	8824	HG23	VAL E	68	14.560	45.169	−27.891		133.82	H
ATOM	8825	N	PRO E	69	12.187	46.769	−25.710		121.06	N
ATOM	8826	CA	PRO E	69	12.539	48.190	−25.618		124.69	C
ATOM	8827	C	PRO E	69	14.021	48.401	−25.907		122.26	C
ATOM	8828	O	PRO E	69	14.823	47.522	−25.593		119.66	O
ATOM	8829	CB	PRO E	69	12.198	48.553	−24.168		120.34	C
ATOM	8830	CG	PRO E	69	11.276	47.473	−23.698		122.90	C
ATOM	8831	CD	PRO E	69	11.689	46.241	−24.428		124.19	C
ATOM	8832	HA	PRO E	69	12.002	48.721	−26.227		129.63	H
ATOM	8833	HB2	PRO E	69	13.009	48.566	−23.636		124.40	H
ATOM	8834	HB3	PRO E	69	11.756	49.416	−24.142		124.40	H
ATOM	8835	HG2	PRO E	69	11.377	47.353	−22.741		127.48	H
ATOM	8836	HG3	PRO E	69	10.361	47.709	−23.918		127.48	H
ATOM	8837	HD2	PRO E	69	12.400	45.786	−23.949		129.03	H
ATOM	8838	HD3	PRO E	69	10.926	45.661	−24.573		129.03	H
ATOM	8839	N	THR E	70	14.370	49.538	−26.499		124.37	N
ATOM	8840	CA	THR E	70	15.756	49.821	−26.866		129.94	C
ATOM	8841	C	THR E	70	16.152	51.237	−26.484		129.58	C
ATOM	8842	O	THR E	70	15.305	52.123	−26.385		129.43	O
ATOM	8843	CB	THR E	70	15.997	49.653	−28.383		131.13	C
ATOM	8844	OG	THR E	70	15.358	50.722	−29.092		133.21	O
ATOM	8845	CG2	THR E	70	15.456	48.325	−28.879		133.64	C
ATOM	8846	H	THR E	70	13.820	50.168	−26.701		129.24	H
ATOM	8847	HA	THR E	70	16.341	49.205	−26.396		135.92	H
ATOM	8848	HB	THR E	70	16.951	49.677	−28.560		137.36	H
ATOM	8849	HG1	THR E	70	15.486	50.636	−29.918		139.85	H
ATOM	8850	HG21	THR E	70	15.615	48.237	−29.832		140.36	H
ATOM	8851	HG22	THR E	70	15.895	47.594	−28.417		140.36	H
ATOM	8852	HG23	THR E	70	14.501	48.274	−28.713		140.36	H
ATOM	8853	N	SER E	71	17.447	51.439	−26.274		128.05	N
ATOM	8854	CA	SER E	71	17.991	52.775	−26.086		133.59	C
ATOM	8855	C	SER E	71	18.133	53.456	−27.445		132.14	C
ATOM	8856	O	SER E	71	18.290	54.673	−27.528		134.41	O
ATOM	8857	CB	SER E	71	19.339	52.713	−25.369		130.01	C
ATOM	8858	OG	SER E	71	20.249	51.897	−26.084		138.73	O
ATOM	8859	H	SER E	71	18.036	50.813	−26.236		133.66	H
ATOM	8860	HA	SER E	71	17.379	53.298	−25.543		140.31	H
ATOM	8861	HB2	SER E	71	19.703	53.610	−25.303		136.01	H
ATOM	8862	HB3	SER E	71	19.209	52.342	−24.483		136.01	H
ATOM	8863	HG	SER E	71	20.986	51.869	−25.682		146.48	H
ATOM	8864	N	THR E	72	18.084	52.655	−28.507		129.50	N
ATOM	8865	CA	THR E	72	18.097	53.166	−29.873		129.84	C
ATOM	8866	C	THR E	72	16.844	54.008	−30.118		128.11	C
ATOM	8867	O	THR E	72	15.733	53.480	−30.080		128.11	O
ATOM	8868	CB	THR E	72	18.157	52.014	−30.900		132.89	C
ATOM	8869	OG1	THR E	72	19.282	51.168	−30.614		137.51	O
ATOM	8870	CG2	THR E	72	18.275	52.554	−32.320		135.87	C
ATOM	8871	H	THR E	72	18.043	51.797	−28.459		135.40	H
ATOM	8872	HA	THR E	72	18.875	53.730	−30.000		135.81	H
ATOM	8873	HB	THR E	72	17.342	51.491	−30.841		139.47	H
ATOM	8874	HG1	THR E	72	19.318	50.540	−31.171		145.01	H
ATOM	8875	HG21	THR E	72	18.312	51.820	−32.952		143.05	H
ATOM	8876	HG22	THR E	72	17.507	53.110	−32.527		143.05	H
ATOM	8877	HG23	THR E	72	19.082	53.086	−32.406		143.05	H
ATOM	8878	N	PRO E	73	17.014	55.318	−30.378		133.46	N
ATOM	8879	CA	PRO E	73	15.854	56.220	−30.408		132.41	C
ATOM	8880	C	PRO E	73	14.911	56.022	−31.595		126.60	C
ATOM	8881	O	PRO E	73	13.739	56.379	−31.482		130.39	O
ATOM	8882	CB	PRO E	73	16.497	57.609	−30.470		129.80	C
ATOM	8883	CG	PRO E	73	17.797	57.390	−31.135		129.20	C
ATOM	8884	CD	PRO E	73	18.267	56.028	−30.697		134.72	C
ATOM	8885	HA	PRO E	73	15.349	56.141	−29.584		138.89	H
ATOM	8886	HB2	PRO E	73	15.939	58.206	−30.993		135.76	H
ATOM	8887	HB3	PRO E	73	16.623	57.953	−29.572		135.76	H
ATOM	8888	HG2	PRO E	73	17.677	57.415	−32.097		135.04	H
ATOM	8889	HG3	PRO E	73	18.425	58.073	−30.852		135.04	H
ATOM	8890	HD2	PRO E	73	18.732	55.582	−31.422		141.67	H
ATOM	8891	HD3	PRO E	73	18.824	56.101	−29.907		141.67	H
ATOM	8892	Z	TYR E	74	15.402	55.472	−32.703		127.41	N
ATOM	8893	CA	TYR E	74	14.567	55.297	−33.890		122.57	C
ATOM	8894	C	TYR E	74	14.741	53.922	−34.522		123.86	C
ATOM	8895	O	TYR E	74	15.859	53.493	−34.810		123.15	O
ATOM	8896	CB	TYR E	74	14.878	56.382	−34.925		123.62	C
ATOM	8897	CG	TYR E	74	13.905	56.415	−36.084		123.55	C
ATOM	8898	CD1	TYR E	74	14.120	55.645	−37.221		121.50	C
ATOM	8899	CD2	TYR E	74	12.770	57.211	−36.038		123.88	C
ATOM	8900	CE1	TYR E	74	13.232	55.673	−38.283		125.17	C
ATOM	8901	CE2	TYR E	74	11.875	57.244	−37.094		127.31	C
ATOM	8902	CZ	TYR E	74	12.112	56.473	−38.214		125.37	C
ATOM	8903	OH	TYR E	74	11.224	56.503	−39.265		128.87	O
ATOM	8904	H	TYR E	74	16.211	55.193	−32.794		132.90	H
ATOM	8905	HA	TYR E	74	13.636	55.390	−33.633		127.09	H
ATOM	8906	HB2	TYR E	74	14.849	57.247	−34.489		128.34	H
ATOM	8907	HB3	TYR E	74	15.765	56.225	−35.286		128.34	H
ATOM	8908	HD1	TYR E	74	14.875	55.105	−37.271		125.80	H
ATOM	8909	HD2	TYR E	74	12.608	57.732	−35.286		128.65	H
ATOM	8910	HE1	TYR E	74	13.390	55.153	−39.038		130.20	H
ATOM	8911	HE2	TYR E	74	11.119	57.784	−37.050		132.77	H
ATOM	8912	HH	TYR E	74	10.592	57.028	−39.092		134.65	H
ATOM	8913	N	GLU E	75	13.616	53.243	−34.736		123.34	N
ATOM	8914	CA	GLU E	75	13.590	51.973	−35.452		122.00	C
ATOM	8915	C	GLU E	75	12.361	51.911	−36.345		122.18	C
ATOM	8916	O	GLU E	75	11.232	52.031	−35.868		122.80	O
ATOM	8917	CB	GLU E	75	13.585	50.783	−34.486		122.49	C
ATOM	8918	CG	GLU E	75	14.930	50.477	−33.863		125.87	C
ATOM	8919	CD	GLU E	75	15.016	49.060	−33.322		131.04	C
ATOM	8920	OE1	GLU E	75	14.083	48.630	−32.606		123.10	O
ATOM	8921	OE2	GLU E	75	16.021	48.375	−33.619		130.63	O1−
ATOM	8922	H	GLU E	75	12.841	53.503	−34.469		128.00	H
ATOM	8923	HA	GLU E	75	14.378	51.906	−36.013		126.40	H
ATOM	8924	HB2	GLU E	75	12.962	50.971	−33.766		126.99	H
ATOM	8925	HB3	GLU E	75	13.297	49.993	−34.970		126.99	H
ATOM	8926	HG2	GLU E	75	15.621	50.584	−34.535		131.05	H
ATOM	8927	HG3	GLU E	75	15.084	51.090	−33.127		131.05	H
ATOM	8928	N	ASP E	76	12.598	51.733	−37.641		118.47	N
ATOM	8929	CA	ASP E	76	11.532	51.564	−38.616		121.95	C
ATOM	8930	C	ASP E	76	11.628	50.178	−39.234		116.59	C
ATOM	8931	O	ASP E	76	12.632	49.831	−39.851		116.66	O
ATOM	8932	CB	ASP E	76	11.610	52.637	−39.701		119.62	C
ATOM	8933	CG	ASP E	76	10.424	52.599	−40.638		125.99	C
ATOM	8934	OD1	ASP E	76	9.322	53.005	−40.215		130.46	O
ATOM	8935	OD2	ASP E	76	10.590	52.164	−41.797		134.44	O1−
ATOM	8936	H	ASP E	76	13.386	51.706	−37.984		122.16	H
ATOM	8937	HA	ASP E	76	10.674	51.641	−38.171		126.34	H
ATOM	8938	HB2	ASP E	76	11.634	53.511	−39.282		123.54	H
ATOM	8939	HB3	ASP E	76	12.413	52.498	−40.227		123.54	H
ATOM	8940	N	LEU E	77	10.574	49.392	−39.056		115.41	N
ATOM	8941	CA	LEU E	77	10.537	48.025	−39.553		116.17	C
ATOM	8942	C	LEU E	77	9.455	47.893	−40.609		115.56	C
ATOM	8943	O	LEU E	77	8.319	48.306	−40.388		117.25	O
ATOM	8944	CB	LEU E	77	10.286	47.048	−38.405		115.28	C
ATOM	8945	CG	LEU E	77	11.389	46.987	−37.350		116.96	C
ATOM	8946	CD1	LEU E	77	10.879	46.320	−36.093		121.16	C
ATOM	8947	CD2	LEU E	77	12.592	46.234	−37.902		119.76	C
ATOM	8948	H	LEU E	77	9.858	49.631	−38.643		118.50	H
ATOM	8949	HA	LEU E	77	11.390	47.807	−39.960		119.40	H
ATOM	8950	HB2	LEU E	77	9.466	47.305	−37.955		118.34	H
ATOM	8951	HB3	LEU E	77	10.188	46.157	−38.775		118.34	H
ATOM	8952	HG	LEU E	77	11.669	47.888	−37.126		120.35	H
ATOM	8953	HD11	LEU E	77	11.594	46.292	−35.438		125.39	H
ATOM	8954	HD12	LEU E	77	10.131	46.831	−35.746		125.39	H
ATOM	8955	HD13	LEU E	77	10.593	45.418	−36.309		125.39	H
ATOM	8956	HD21	LEU E	77	13.284	46.203	−37.223		123.72	H
ATOM	8957	HD22	LEU E	77	12.319	45.333	−38.138		123.72	H
ATOM	8958	HD23	LEU E	77	12.921	46.697	−38.689		123.72	H
ATOM	8959	N	THR E	78	9.813	47.329	−41.759		114.27	N
ATOM	8960	CA	THR E	78	8.840	47.089	−42.818		114.26	C
ATOM	8961	C	THR E	78	8.861	45.634	−43.248		114.87	C
ATOM	8962	O	THR E	78	9.922	45.020	−43.355		112.85	O
ATOM	8963	CB	THR E	78	9.100	47.973	−44.050		115.27	C
ATOM	8964	OG1	THR E	78	9.102	49.353	−43.665		119.62	O
ATOM	8965	CG2	THR E	78	8.035	47.754	−45.113		115.91	C
ATOM	8966	H	THR E	78	10.612	47.075	−41.950		117.12	H
ATOM	8967	HA	THR E	78	7.952	47.292	−42.484		117.11	H
ATOM	8968	HB	THR E	78	9.962	47.746	−44.431		118.32	H
ATOM	8969	HG1	THR E	78	9.704	49.491	−43.096		123.54	H
ATOM	8970	HG21	THR E	78	8.213	48.317	−45.882		119.09	H
ATOM	8971	HG22	THR E	78	8.035	46.826	−45.396		119.09	H
ATOM	8972	HG23	THR E	78	7.160	47.974	−44.757		119.09	H
ATOM	8973	N	TYR E	79	7.670	45.095	−43.484		113.27	N
ATOM	8974	CA	TYR E	79	7.514	43.775	−44.072		114.20	C
ATOM	8975	C	TYR E	79	6.573	43.872	−45.256		114.36	C
ATOM	8976	0	TYR E	79	5.421	44.279	−45.111		113.68	O
ATOM	8977	CB	TYR E	79	6.982	42.777	−43.049		113.72	C
ATOM	8978	CG	TYR E	79	6.699	41.404	−43.618		114.03	C
ATOM	8979	CD1	TYR E	79	7.700	40.665	−44.239		115.69	C
ATOM	8980	CD2	TYR E	79	5.438	40.835	−43.512		113.78	C
ATOM	8981	CE1	TYR E	79	7.447	39.401	−44.750		115.27	C
ATOM	8982	CE2	TYR E	79	5.177	39.579	−44.016		112.76	C
ATOM	8983	CZ	TYR E	79	6.182	38.865	−44.635		115.58	C
ATOM	8984	OH	TYR E	79	5.914	37.609	−45.136		114.38	O
ATOM	8985	H	TYR E	79	6.924	45.484	−43.308		115.93	H
ATOM	8986	HA	TYR E	79	8.375	43.460	−44.390		117.04	H
ATOM	8987	HB2	TYR E	79	7.638	42.675	−42.342		116.47	H
ATOM	8988	HB3	TYR E	79	6.153	43.120	−42.681		116.47	H
ATOM	8989	HD1	TYR E	79	8.553	41.027	−44.317		118.83	H
ATOM	8990	HD2	TYR E	79	4.756	41.311	−43.096		116.54	H
ATOM	8991	HE1	TYR E	79	8.124	38.920	−45.167		118.32	H
ATOM	8992	HE2	TYR E	79	4.325	39.215	−43.940		115.31	H
ATOM	8993	HH	TYR E	79	6.606	37.285	−45.484		117.25	H
ATOM	8994	N	PHE E	80	7.078	43.501	−46.426		113.15	N
ATOM	8995	CA	PHE E	80	6.317	43.575	−47.664		114.24	C
ATOM	8996	C	PHE E	80	6.024	42.162	−48.125		116.30	C
ATOM	8997	O	PHE E	80	6.934	41.349	−48.213		115.43	O
ATOM	8998	CB	PHE E	80	7.102	44.352	−48.722		117.01	C
ATOM	8999	CG	PHE E	80	6.447	44.383	−50.071		119.40	C
ATOM	9000	CD1	PHE E	80	5.421	45.272	−50.337		118.32	C
ATOM	9001	CD2	PHE E	80	6.877	43.541	−51.084		119.37	C
ATOM	9002	CE1	PHE E	80	4.824	45.310	−51.585		123.34	C
ATOM	9003	CE2	PHE E	80	6.285	43.574	−52.334		118.06	C
ATOM	9004	CZ	PHE E	80	5.259	44.459	−52.585		118.37	C
ATOM	9005	H	PHE E	80	7.876	43.197	−46.529		115.78	H
ATOM	9006	HA	PHE E	80	5.476	44.031	−47.504		117.09	H
ATOM	9007	HB2	PHE E	80	7.206	45.269	−48.422		120.41	H
ATOM	9008	HB3	PHE E	80	7.975	43.941	−48.827		120.41	H
ATOM	9009	HD1	PHE E	80	5.125	45.846	−49.668		121.98	H
ATOM	9010	HD2	PHE E	80	7.569	42.942	−50.920		123.25	H
ATOM	9011	HE1	PHE E	80	4.13	45.908	−51.751		128.00	H
ATOM	9012	HE2	PHE E	80	6.579	43.000	−53.004		121.67	H
ATOM	9013	HZ	PHE E	80	4.858	44.482	−53.424		122.04	H
ATOM	9014	N	TYR E	81	4.751	41.864	−48.376		113.87	N
ATOM	9015	CA	TYR E	81	4.354	40.551	−48.870		115.55	C
ATOM	9016	C	TYR E	81	3.404	40.698	−50.049		117.93	C
ATOM	9017	O	TYR E	81	2.378	41.378	−49.952		114.45	O
ATOM	9018	CB	TYR E	81	3.696	39.715	−47.768		113.17	C
ATOM	9019	CG	TYR E	81	3.300	38.345	−48.261		115.78	C
ATOM	9020	CD1	TYR E	81	4.237	37.324	−48.352		119.61	C
ATOM	9021	CD2	TYR E	81	1.998	38.077	−48.663		118.88	C
ATOM	9022	CE1	TYR E	81	3.887	36.072	−48.816		119.41	C
ATOM	9023	CE2	TYR E	81	1.640	36.827	−49.130		117.69	C
ATOM	9024	CZ	TYR E	81	2.586	35.829	−49.203		117.85	C
ATOM	9025	OH	TYR E	81	2.237	34.580	−49.670		117.84	O
ATOM	9026	H	TYR E	81	4.095	42.409	−48.267		116.64	H
ATOM	9027	HA	TYR E	81	5.143	40.076	−49.177		118.66	H
ATOM	9028	HB2	TYR E	81	4.322	39.604	−47.036		115.81	H
ATOM	9029	HB3	TYR E	81	2.897	40.169	−47.459		115.81	H
ATOM	9030	HD1	TYR E	81	5.115	37.485	−48.092		123.54	H
ATOM	9031	HD2	TYR E	81	1.357	38.749	−48.615		122.66	H
ATOM	9032	HE1	TYR E	81	4.525	35.397	−48.868		123.29	H
ATOM	9033	HE2	TYR E	81	0.763	36.660	−49.392		121.22	H
ATOM	9034	HH	TYR E	81	1.421	34.566	−49.870		121.41	H
ATOM	9035	N	GLU E	82	3.755	40.055	−51.159		115.98	N
ATOM	9036	CA	GLU E	82	3.003	40.184	−52.399		114.65	C
ATOM	9037	C	GLU E	82	2.789	38.829	−53.047		114.84	C
ATOM	9038	O	GLU E	82	3.732	38.055	−53.188		117.94	O
ATOM	9039	CB	GLU E	82	3.737	41.109	−53.373		118.04	C
ATOM	9040	CG	GLU E	82	3.018	41.338	−54.689		116.30	C
ATOM	9041	CD	GLU E	82	3.879	42.074	−55.695		122.72	C
ATOM	9042	OE1	GLU E	82	4.616	41.397	−56.440		120.02	O
ATOM	9043	OE2	GLU E	82	3.824	43.322	−55.736		120.27	O1−
ATOM	9044	H	GLU E	82	4.434	39.531	−51.219		119.17	H
ATOM	9045	HA	GLU E	82	2.134	40.571	−52.208		117.57	H
ATOM	9046	HB2	GLU E	82	3.857	41.974	−52.949		121.64	H
ATOM	9047	HB3	GLU E	82	4.604	40.722	−53.575		121.64	H
ATOM	9048	HG2	GLU E	82	2.774	40.481	−55.071		119.56	H
ATOM	9049	HG3	GLU E	82	2.223	41.870	−54.527		119.56	H
ATOM	9050	N	CYS E	83	1.547	38.545	−53.433		115.34	N
ATOM	9051	CA	CYS E	83	1.264	37.378	−54.257		112.96	C
ATOM	9052	C	CYS E	83	0.843	37.867	−55.639		119.15	C
ATOM	9053	O	CYS E	83	0.264	38.947	−55.785		115.77	O
ATOM	9054	CB	CYS E	83	0.197	36.477	−53.621		116.84	C
ATOM	9055	SG	CYS E	83	−1.483	37.137	−53.496		123.13	S
ATOM	9056	H	CYS E	83	0.854	39.012	−53.230		118.41	H
ATOM	9057	HA	CYS E	83	2.076	36.857	−54.357		115.56	H
ATOM	9058	HB2	CYS E	83	0.144	35.661	−54.142		120.21	H
ATOM	9059	HB3	CYS E	83	0.486	36.260	−52.720		120.21	H
ATOM	9060	N	ASP E	84	1.163	37.066	−56.648		117.04	N
ATOM	9061	CA	ASP E	84	0.974	37.441	−58.041		117.78	C
ATOM	9062	C	ASP E	84	0.295	36.299	−58.783		119.08	C
ATOM	9063	O	ASP E	84	0.770	35.164	−58.744		116.97	O
ATOM	9064	CB	ASP E	84	2.325	37.778	−58.678		120.88	C
ATOM	9065	CG	ASP E	84	2.208	38.205	−60.131		125.61	C
ATOM	9066	OD1	ASP E	84	1.845	37.363	−60.982		120.93	O
ATOM	9067	OD2	ASP E	84	2.505	39.382	−60.423		120.27	O1−
ATOM	9068	H	ASP E	84	1.500	36.281	−56.547		120.45	H
ATOM	9069	HA	ASP E	84	0.405	38.224	−58.092		121.34	H
ATOM	9070	HB2	ASP E	84	2.734	38.506	−58.184		125.05	H
ATOM	9071	HB3	ASP E	84	2.895	36.993	−58.642		125.05	H
ATOM	9072	N	TYR E	85	−0.824	36.598	−59.437		118.50	N
ATOM	9073	CA	TYR E	85	−1.525	35.609	−60.252		119.06	C
ATOM	9074	C	TYR E	85	−1.499	36.041	−61.713		120.41	C
ATOM	9075	O	TYR E	85	2.219	36.955	−62.124		120.32	O
ATOM	9076	CB	TYR E	85	−2.960	35.422	−59.768		118.28	C
ATOM	9077	CG	TYR E	85	3.596	34.138	−60.246		118.94	C
ATOM	9078	CD1	TYR E	85	−3.038	32.910	−59.929		119.95	C
ATOM	9079	CD2	TYR E	85	−4.760	34.154	−61.002		123.18	C
ATOM	9080	CE1	TYR E	85	−3.613	31.733	−60.354		120.65	C
ATOM	9081	CE2	TYR E	85	5.345	32.979	−61.430		125.96	C
ATOM	9082	CZ	TYR E	85	−4.767	31.772	−61.099		123.05	C
ATOM	9083	OH	TYR E	85	−5.337	30.594	−61.524		126.20	O
ATOM	9084	H	TYR E	85	−1.201	37.371	−59.426		122.20	H
ATOM	9085	HA	TYR E	85	−1.068	34.757	−60.180		122.87	H
ATOM	9086	HB2	TYR E	85	2.965	35.412	−58.798		121.94	H
ATOM	9087	HB3	TYR E	85	−3.499	36.160	−60.093		121.94	H
ATOM	9088	HD1	TYR E	85	−2.259	32.880	−59.422		123.94	H
ATOM	9089	HD2	TYR E	85	−5.152	34.968	−61.222		127.82	H
ATOM	9090	HE1	TYR E	85	−3.226	30.917	−60.134		124.78	H
ATOM	9091	HE2	TYR E	85	−6.124	33.002	−61.937		131.15	H
ATOM	9092	HH	TYR E	85	−6.033	30.755	−61.966		131.44	H
ATOM	9093	N	THR E	86	−0.648	35.368	−62.481		121.39	N
ATOM	9094	CA	THR E	86	−0.390	35.705	−63.874		120.93	C
ATOM	9095	C	THR E	86	−0.293	34.414	−64.674		121.34	C
ATOM	9096	O	THR E	86	0.496	33.532	−64.334		119.84	O
ATOM	9097	CB	THR E	86	0.921	36.515	−64.029		122.67	C
ATOM	9098	OG1	THR E	86	0.862	37.696	−63.217		124.63	O
ATOM	9099	CG2	THR E	86	1.149	36.917	−65.478		123.65	C
ATOM	9100	H	THR E	86	−0.196	34.690	−62.206		125.66	H
ATOM	9101	HA	THR E	86	−1.125	36.233	−64.223		125.12	H
ATOM	9102	HB	THR E	86	1.670	35.969	−63.744		127.20	H
ATOM	9103	HG1	THR E	86	0.765	37.485	−62.410		129.56	H
ATOM	9104	HG21	THR E	86	1.973	37.423	−65.555		128.38	H
ATOM	9105	HG22	THR E	86	1.212	36.126	−66.035		128.38	H
ATOM	9106	HG23	THR E	86	0.412	37.466	−65.790		128.38	H
ATOM	9107	N	ASP E	87	−1.096	34.300	−65.727		122.89	N
ATOM	9108	CA	ASP E	87	−1.097	33.101	−66.563		123.19	C
ATOM	9109	C	ASP E	87	−1.404	31.876	−65.703		126.71	C
ATOM	9110	O	ASP E	87	−0.771	30.830	−65.835		123.26	O
ATOM	9111	CB	ASP E	87	0.252	32.946	−67.275		125.03	C
ATOM	9112	CG	ASP E	87	0.247	31.838	−68.316		128.16	C
ATOM	9113	OD1	ASP E	87	−0.798	31.626	−68.965		124.41	O
ATOM	9114	OD2	ASP E	87	1.295	31.180	−68.478		126.54	O1−
ATOM	9115	H	ASP E	87	−1.653	34.904	−65.981		127.47	H
ATOM	9116	HA	ASP E	87	−1.789	33.181	−67.237		127.83	H
ATOM	9117	HB2	ASP E	87	0.469	33.778	−67.725		130.03	H
ATOM	9118	HB3	ASP E	87	0.934	32.737	−66.618		130.03	H
ATOM	9119	N	ASN E	88	−2.372	32.032	−64.803		129.28	N
ATOM	9120	CA	ASN E	88	−2.802	30.961	−63.906		125.51	C
ATOM	9121	C	ASN E	88	−1.681	30.405	−63.031		123.64	C
ATOM	9122	O	ASN E	88	−1.812	29.322	−62.465		124.76	O
ATOM	9123	CB	ASN E	88	−3.430	29.821	−64.709		129.13	C
ATOM	9124	CG	ASN E	88	−4.619	30.277	−65.532		135.20	C
ATOM	9125	OD1	ASN E	88	−4.620	30.161	−66.757		140.38	O
ATOM	9126	ND2	ASN E	88	5.637	30.804	−64.860		137.30	N
ATOM	9127	H	ASN E	88	−2.804	32.767	−64.690		135.13	H
ATOM	9128	HA	ASN E	88	−3.486	31.313	−63.314		130.61	H
ATOM	9129	HB2	ASN E	88	−2.766	29.457	−65.316		134.96	H
ATOM	9130	HB3	ASN E	88	−3.735	29.133	−64.097		134.96	H
ATOM	9131	HD21	ASN E	88	−6.335	31.078	−65.282		144.76	H
ATOM	9132	HD22	ASN E	88	−5.599	30.871	−64.004		144.76	H
ATOM	9133	N	LYS E	89	−0.585	31.150	−62.920		120.99	N
ATOM	9134	CA	LYS E	89	0.543	30.745	−62.087		122.61	C
ATOM	9135	C	LYS E	89	0.681	31.653	−60.868		118.77	C
ATOM	9136	O	LYS E	89	0.632	32.882	−60.978		117.15	O
ATOM	9137	CB	LYS E	89	1.835	30.748	−62.902		124.56	C
ATOM	9138	CG	LYS E	89	1.924	29.593	−63.887		135.41	C
ATOM	9139	CD	LYS E	89	3.119	29.732	−64.818		145.55	C
ATOM	9140	CE	LYS E	89	3.242	28.527	−65.737		146.80	C
ATOM	9141	NZ	LYS E	89	1.975	28.255	−66.473		149.89	N1+
ATOM	9142	H	LYS E	89	−0.469	31.902	−63.320		125.19	H
ATOM	9143	HA	LYS E	89	0.391	29.841	−61.770		127.14	H
ATOM	9144	HB2	LYS E	89	1.888	31.575	−63.406		129.48	H
ATOM	9145	HB3	LYS E	89	2.590	30.682	−62.296		129.48	H
ATOM	9146	HG2	LYS E	89	2.018	28.762	−63.396		142.50	H
ATOM	9147	HG3	LYS E	89	1.120	29.573	−64.428		142.50	H
ATOM	9148	HD2	LYS E	89	3.008	30.524	−65.367		154.66	H
ATOM	9149	HD3	LYS E	89	3.930	29.799	−64.291		154.66	H
ATOM	9150	HE2	LYS E	89	3.941	28.695	−66.389		156.16	H
ATOM	9151	HE3	LYS E	89	3.459	27.744	−65.207		156.16	H
ATOM	9152	HZ1	LYS E	89	1.755	28.959	−66.971		159.87	H
ATOM	9153	HZ2	LYS E	89	2.077	27.546	−67.001		159.87	H
ATOM	9154	HZ3	LYS E	89	1.317	28.093	−65.895		159.87	H
ATOM	9155	N	SER E	90	0.843	31.024	−59.709		116.33	N
ATOM	9156	CA	SER E	90	0.971	31.729	−58.442		117.73	C
ATOM	9157	C	SER E	90	2.439	31.908	−58.084		118.63	C
ATOM	9158	O	SER E	90	3.171	30.928	−57.975		117.42	O
ATOM	9159	CB	SER E	90	0.257	30.961	−57.328		117.54	C
ATOM	9160	OG	SER E	90	−1.103	30.730	−57.645		120.05	O
ATOM	9161	H	SER E	90	0.883	30.169	−59.631		119.60	H
ATOM	9162	HA	SER E	90	0.565	32.607	−58.518		121.27	H
ATOM	9163	HB2	SER E	90	0.699	30.107	−57.203		121.05	H
ATOM	9164	HB3	SER E	90	0.305	31.479	−56.509		121.05	H
ATOM	9165	HG	SER E	90	−1.501	31.461	−57.755		124.06	H
ATOM	9166	N	THR E	91	2.864	33.157	−57.912		117.55	N
ATOM	9167	CA	THR E	91	4.222	33.455	−57.473		114.99	C
ATOM	9168	C	THR E	91	4.178	34.462	−56.329		120.38	C
ATOM	9169	O	THR E	91	3.207	35.208	−56.177		119.44	O
ATOM	9170	CB	THR E	91	5.096	34.001	−58.621		118.36	C
ATOM	9171	OG1	THR E	91	4.482	35.159	−59.191		117.75	O
ATOM	9172	CG2	THR E	91	5.280	32.946	−59.702		121.31	C
ATOM	9173	H	THR E	91	2.379	33.855	−58.045		121.06	H
ATOM	9174	HA	THR E	91	4.634	32.641	−57.142		117.98	H
ATOM	9175	HB	THR E	91	5.971	34.239	−58.274		122.03	H
ATOM	9176	HG1	THR E	91	4.394	35.756	−58.607		121.30	H
ATOM	9177	HG21	THR E	91	5.830	33.299	−60.419		125.58	H
ATOM	9178	HG22	THR E	91	5.712	32.161	−59.329		125.58	H
ATOM	9179	HG23	THR E	91	4.417	32.689	−60.064		125.58	H
ATOM	9180	N	PHE E	92	5.232	34.465	−55.523		117.07	N
ATOM	9181	CA	PHE E	92	5.250	35.231	−54.287		119.25	C
ATOM	9182	C	PHE E	92	6.563	35.971	−54.119		124.03	C
ATOM	9183	O	PHE E	92	7.601	35.561	−54.641		120.37	O
ATOM	9184	CB	PHE E	92	5.015	34.308	−53.091		118.30	C
ATOM	9185	CG	PHE E	92	3.758	33.502	−53.192		120.97	C
ATOM	9186	CD1	PHE E	92	2.557	34.006	−52.722		119.39	C
ATOM	9187	CD2	PHE E	92	3.773	32.244	−53.771		124.13	C
ATOM	9188	CE1	PHE E	92	1.397	33.266	−52.819		118.89	C
ATOM	9189	CE2	PHE E	92	2.616	31.498	−53.871		117.65	C
ATOM	9190	CZ	PHE E	92	1.426	32.010	−53.395		124.23	C
ATOM	9191	H	PHE E	92	5.957	34.027	−55.672		120.48	H
ATOM	9192	HA	PHE E	92	4.535	35.885	−54.308		123.10	H
ATOM	9193	HB2	PHE E	92	5.760	33.690	−53.022		121.96	H
ATOM	9194	HB3	PHE E	92	4.959	34.846	−52.287		121.96	H
ATOM	9195	HD1	PHE E	92	2.533	34.850	−52.333		123.27	H
ATOM	9196	HD2	PHE E	92	4.573	31.895	−54.092		128.95	H
ATOM	9197	HE1	PHE E	92	0.596	33.612	−52.498		122.66	H
ATOM	9198	HE2	PHE E	92	2.638	30.653	−54.259		121.19	H
ATOM	9199	HZ	PHE E	92	0.644	31.510	−53.461		129.08	H
ATOM	9200	N	ASP E	93	6.497	37.065	−53.374		120.31	N
ATOM	9201	CA	ASP E	93	7.647	37.915	−53.135		122.87	C
ATOM	9202	C	ASP E	93	7.507	38.528	−51.752		121.59	C
ATOM	9203	O	ASP E	93	6.409	38.918	−51.354		120.77	O
ATOM	9204	CB	ASP E	93	7.743	39.002	−54.211		124.57	C
ATOM	9205	CG	ASP E	93	8.998	39.840	−54.085		132.86	C
ATOM	9206	OD1	ASP E	93	9.991	39.332	−53.526		132.28	O1−
ATOM	9207	OD2	ASP E	93	8.994	41.002	−54.550		130.92	O
ATOM	9208	H	ASP E	93	5.779	37.340	−52.989		124.37	H
ATOM	9209	HA	ASP E	93	8.458	37.382	−53.158		127.44	H
ATOM	9210	HB2	ASP E	93	7.748	38.582	−55.085		129.48	H
ATOM	9211	HB3	ASP E	93	6.978	39.594	−54.131		129.48	H
ATOM	9212	N	GLN E	94	8.60	38.592	−51.005		121.93	N
ATOM	9213	CA	GLN E	94	8.567	39.269	−49.718		121.60	C
ATOM	9214	C	GLN E	94	9.897	39.936	−49.420		125.96	C
ATOM	9215	O	GLN E	94	10.960	39.425	−49.778		122.95	O
ATOM	9216	CB	GLN E	94	8.184	38.298	−48.590		118.61	C
ATOM	9217	CG	GLN E	94	9.153	37.149	−48.353		122.48	C
ATOM	9218	CD	GLN E	94	8.735	36.253	−47.190		131.39	C
ATOM	9219	OE1	GLN E	94	7.596	36.309	−46.716		122.85	O
ATOM	9220	NE2	GLN E	94	9.662	35.422	−46.724		133.95	N
ATOM	9221	H	GLN E	94	9.365	38.258	−51.217		126.32	H
ATOM	9222	HA	GLN E	94	7.890	39.963	−49.750		125.92	H
ATOM	9223	HB2	GLN E	94	8.120	38.800	−47.762		122.33	H
ATOM	9224	HB3	GLN E	94	7.320	37.910	−48.799		122.33	H
ATOM	9225	HG2	GLN E	94	9.197	36.603	−49.153		126.97	H
ATOM	9226	HG3	GLN E	94	10.030	37.513	−48.151		126.97	H
ATOM	9227	HE21	GLN E	94	9.478	34.895	−46.070		140.74	H
ATOM	9228	HE22	GLN E	94	10.446	35.411	−47.078		140.74	H
ATOM	9229	N	ASP E	95	9.812	41.095	−48.774		119.56	N
ATOM	9230	CA	ASP E	95	10.979	41.896	−48.435		123.21	C
ATOM	9231	C	ASP E	95	10.903	42.330	−46.983		120.85	C
ATOM	9232	O	ASP E	95	9.814	42.501	−46.431		116.26	O
ATOM	9233	CB	ASP E	95	11.077	43.129	−49.338		122.27	C
ATOM	9234	CG	ASP E	95	11.333	42.774	−50.787		129.57	C
ATOM	9235	OD1	ASP E	95	12.132	41.848	−51.043		135.45	O
ATOM	9236	OD2	ASP E	95	10.733	43.425	−51.668		131.38	O1−
ATOM	9237	H	ASP E	95	9.070	41.446	−48.517		123.47	H
ATOM	9238	HA	ASP E	95	11.781	41.364	−48.554		127.85	H
ATOM	9239	HB2	ASP E	95	10.242	43.621	−49.293		126.72	H
ATOM	9240	HB3	ASP E	95	11.808	43.687	−49.032		126.72	H
ATOM	9241	N	TYR E	96	12.072	42.504	−46.380		115.26	N
ATOM	9242	CA	TYR E	96	12.200	43.027	−45.028		116.09	C
ATOM	9243	C	TYR E	96	13.083	44.268	−45.060		118.85	C
ATOM	9244	O	TYR E	96	14.186	44.218	−45.609		118.14	O
ATOM	9245	CB	TYR E	96	12.814	41.990	−44.091		117.29	C
ATOM	9246	CG	TYR E	96	12.171	40.625	−44.131		119.72	C
ATOM	9247	CD1	TYR E	96	12.520	39.700	−45.108		119.79	C
ATOM	9248	CD2	TYR E	96	11.234	40.250	−43.177		118.62	C
ATOM	9249	CE1	TYR E	96	11.944	38.446	−45.140		122.85	C
ATOM	9250	CE2	TYR E	96	10.652	38.999	−43.201		120.70	C
ATOM	9251	CZ	TYR E	96	11.012	38.099	−44.185		120.85	C
ATOM	9252	OH	TYR E	96	10.437	36.849	−44.213		124.95	O
ATOM	9253	H	TYR E	96	12.828	42.319	−46.746		118.31	H
ATOM	9254	HA	TYR E	96	11.326	43.275	−44.688		119.31	H
ATOM	9255	HB2	TYR E	96	13.749	41.879	−44.325		120.75	H
ATOM	9256	HB3	TYR E	96	12.745	42.318	−43.181		120.75	H
ATOM	9257	HD1	TYR E	96	13.149	39.930	−45.753		123.75	H
ATOM	9258	HD2	TYR E	96	10.992	40.855	−42.513		122.34	H
ATOM	9259	HE1	TYR E	96	12.184	37.838	−45.801		127.42	H
ATOM	9260	HE2	TYR E	96	10.024	38.762	−42.558		124.84	H
ATOM	9261	HH	TYR E	96	9.891	36.770	−43.580		129.94	H
ATOM	9262	N	LEU E	97	12.606	45.365	−44.474		114.66	N
ATOM	9263	CA	LEU E	97	13.385	46.602	−44.404		120.71	C
ATOM	9264	C	LEU E	97	13.605	47.025	−42.961		117.15	C
ATOM	9265	O	LEU E	97	12.681	46.998	−42.143		115.93	O
ATOM	9266	CB	LEU E	97	12.698	47.752	−45.151		118.74	C
ATOM	9267	CG	LEU E	97	12.170	47.515	−46.563		124.83	C
ATOM	9268	CD1	LEU E	97	11.391	48.729	−47.041		131.08	C
ATOM	9269	CD2	LEU E	97	13.316	47.219	−47.496		124.75	C
ATOM	9270	H	LEU E	97	11.831	45.420	−44.106		117.60	H
ATOM	9271	HA	LEU E	97	14.253	46.453	−44.811		124.85	H
ATOM	9272	HB2	LEU E	97	11.942	48.039	−44.617		122.48	H
ATOM	9273	HB3	LEU E	97	13.334	48.482	−45.212		122.48	H
ATOM	9274	HG	LEU E	97	11.574	46.750	−46.559		129.80	H
ATOM	9275	HD11	LEU E	97	11.064	48.560	−47.938		137.30	H
ATOM	9276	HD12	LEU E	97	10.645	48.881	−46.440		137.30	H
ATOM	9277	HD13	LEU E	97	11.979	49.500	−47.043		137.30	H
ATOM	9278	HD21	LEU E	97	12.965	47.071	−48.388		129.70	H
ATOM	9279	HD22	LEU E	97	13.923	47.976	−47.500		129.70	H
ATOM	9280	HD23	LEU E	97	13.778	46.425	−47.186		129.70	H
ATOM	9281	N	TYR E	98	14.840	47.417	−42.665		115.72	N
ATOM	9282	CA	TYR E	98	15.182	48.046	−41.401		118.67	C
ATOM	9283	C	TYR E	98	15.675	49.456	−41.704		122.10	C
ATOM	9284	O	TYR E	98	16.701	49.630	−42.363		118.15	O
ATOM	9285	CB	TYR E	98	16.247	47.242	−40.655		119.19	C
ATOM	9286	CG	TYR E	98	16.571	47.797	−39.287		123.54	C
ATOM	9287	CD1	TYR E	98	17.573	48.742	−39.119		125.80	C
ATOM	9288	CD2	TYR E	98	15.864	47.387	−38.165		122.25	C
ATOM	9289	CE1	TYR E	98	17.866	49.257	−37.872		124.47	C
ATOM	9290	CE2	TYR E	98	16.153	47.895	−36.913		122.72	C
ATOM	9291	CZ	TYR E	98	17.154	48.829	−36.774		126.85	C
ATOM	9292	OH	TYR E	98	17.446	49.337	−35.533		129.33	O
ATOM	9293	H	TYR E	98	15.511	47.325	−43.196		118.86	H
ATOM	9294	HA	TYR E	98	14.392	48.107	−40.843		122.40	H
ATOM	9295	HB2	TYR E	98	15.930	46.333	−40.540		123.03	H
ATOM	9296	HB3	TYR E	98	17.064	47.243	−41.177		123.03	H
ATOM	9297	HD1	TYR E	98	18.056	49.032	−39.859		130.96	H
ATOM	9298	HD2	TYR E	98	15.187	46.755	−38.256		126.70	H
ATOM	9299	HE1	TYR E	98	18.543	49.887	−37.774		129.36	H
ATOM	9300	HE2	TYR E	98	15.674	47.609	−36.169		127.26	H
ATOM	9301	HH	TYR E	98	16.941	48.995	−34.956		135.20	H
ATOM	9302	N	ASN E	99	14.934	50.454	−41.232		119.00	N
ATOM	9303	CA	ASN E	99	15.201	51.846	−41.579		117.34	C
ATOM	9304	C	ASN E	99	15.317	52.027	−43.095		124.69	C
ATOM	9305	O	ASN E	99	16.193	52.735	−43.589		120.15	O
ATOM	9306	CB	ASN E	99	16.465	52.334	−40.868		118.40	C
ATOM	9307	CG	ASN E	99	16.290	52.391	−39.355		118.42	C
ATOM	9308	OD1	ASN E	99	15.170	52.483	−38.856		119.63	O
ATOM	9309	ND2	ASN E	99	17.393	52.334	−38.623		123.08	N
ATOM	9310	H	ASN E	99	14.263	50.350	−40.704		122.81	H
ATOM	9311	HA	ASN E	99	14.460	52.391	−41.272		120.80	H
ATOM	9312	HB2	ASN E	99	17.195	51.726	−41.064		122.08	H
ATOM	9313	HB3	ASN E	99	16.681	53.226	−41.180		122.08	H
ATOM	9314	HD21	ASN E	99	17.342	52.363	−37.765		127.69	H
ATOM	9315	HD22	ASN E	99	18.161	52.269	−39.006		127.69	H
ATOM	9316	N	GLY E	100	14.419	51.373	−43.825		119.11	N
ATOM	9317	CA	GLY E	100	14.309	51.561	−45.260		122.08	C
ATOM	9318	C	GLY E	100	15.283	50.739	−46.080		125.95	C
ATOM	9319	O	GLY E	100	15.210	50.742	−47.308		124.82	O
ATOM	9320	H	GLY E	100	13.856	50.807	−43.505		122.93	H
ATOM	9321	HA2	GLY E	100	13.410	51.329	−45.541		126.49	H
ATOM	9322	HA3	GLY E	100	14.457	52.497	−45.467		126.49	H
ATOM	9323	N	GLU E	101	16.189	50.032	−45.410		123.34	N
ATOM	9324	CA	GLU E	101	17.208	49.242	−46.095		121.40	C
ATOM	9325	C	GLU E	101	16.874	47.756	−46.068		125.31	C
ATOM	9326	O	GLU E	101	16.667	47.178	−44.996		120.68	O
ATOM	9327	CB	GLU E	101	18.576	49.483	−45.457		128.51	C
ATOM	9328	CG	GLU E	101	19.701	48.678	−46.079		136.34	C
ATOM	9329	CD	GLU E	101	21.060	49.064	−45.529		150.28	C
ATOM	9330	OE1	GLU E	101	21.512	50.198	−45.804		153.61	O
ATOM	9331	OE2	GLU E	101	21.673	48.237	−44.819		156.44	O1−
ATOM	9332	H	GLU E	101	16.236	49.993	−44.552		128.01	H
ATOM	9333	HA	GLU E	101	17.255	49.522	−47.022		125.68	H
ATOM	9334	HB2	GLU E	101	18.800	50.422	−45.548		134.21	H
ATOM	9335	HB3	GLU E	101	18.528	49.247	−44.518		134.21	H
ATOM	9336	HG2	GLU E	101	19.558	47.737	−45.893		143.61	H
ATOM	9337	HG3	GLU E	101	19.709	48.831	−47.037		143.61	H
ATOM	9338	N	GLU E	102	16.828	47.141	−47.248		119.84	N
ATOM	9339	CA	GLU E	102	16.530	45.717	−47.360		121.48	C
ATOM	9340	C	GLU E	102	17.575	44.873	−46.653		122.97	C
ATOM	9341	O	GLU E	102	18.764	45.180	−46.681		123.40	O
ATOM	9342	CB	GLU E	102	16.447	45.279	−48.826		128.87	C
ATOM	9343	CG	GLU E	102	15.053	45.320	−49.420		134.38	C
ATOM	9344	CD	GLU E	102	14.891	44.382	−50.604		139.93	C
ATOM	9345	OE1	GLU E	102	14.841	43.150	−50.386		141.37	O
ATOM	9346	OE2	GLU E	102	14.807	44.875	−51.749		149.33	O1−
ATOM	9347	H	GLU E	102	16.968	47.529	−48.003		123.81	H
ATOM	9348	HA	GLU E	102	15.671	45.541	−46.945		125.78	H
ATOM	9349	HB2	GLU E	102	17.009	45.865	−49.357		134.65	H
ATOM	9350	HB3	GLU E	102	16.769	44.367	−48.896		134.65	H
ATOM	9351	HG2	GLU E	102	14.413	45.059	−48.740		141.25	H
ATOM	9352	HG3	GLU E	102	14.866	46.222	−49.724		141.25	H
ATOM	9353	N	TYR E	103	17.121	43.797	−46.025		121.26	N
ATOM	9354	CA	TYR E	103	18.031	42.827	−45.444		120.13	C
ATOM	9355	C	TYR E	103	17.377	41.454	−45.470		120.08	C
ATOM	9356	O	TYR E	103	16.155	41.338	−45.607		118.12	O
ATOM	9357	CB	TYR E	103	18.430	43.236	−44.021		121.72	C
ATOM	9358	CG	TYR E	103	17.330	43.173	−42.978		121.02	C
ATOM	9359	CD1	TYR E	103	16.273	44.078	−42.985		121.46	C
ATOM	9360	CD2	TYR E	103	17.374	42.232	−41.961		119.71	C
ATOM	9361	CE1	TYR E	103	15.279	44.024	−42.020		114.20	C
ATOM	9362	CE2	TYR E	103	16.388	42.171	−40.994		115.96	C
ATOM	9363	CZ	TYR E	103	15.344	43.065	−41.029		114.97	C
ATOM	9364	OH	TYR E	103	14.370	43.002	−40.059		113.45	O
ATOM	9365	H	TYR E	103	16.289	43.607	−45.923		125.51	H
ATOM	9366	HA	TYR E	103	18.837	42.786	−45.982		124.15	H
ATOM	9367	HB2	TYR E	103	19.144	42.651	−43.724		126.06	H
ATOM	9368	HB3	TYR E	103	18.752	44.151	−44.046		126.06	H
ATOM	9369	HD1	TYR E	103	16.226	44.722	−43.654		125.75	H
ATOM	9370	HD2	TYR E	103	18.076	41.623	−41.935		123.65	H
ATOM	9371	HE1	TYR E	103	14.573	44.630	−42.040		117.04	H
ATOM	9372	HE2	TYR E	103	16.430	41.528	−40.324		119.15	H
ATOM	9373	HH	TYR E	103	14.536	42.375	−39.526		116.14	H
ATOM	9374	N	THR E	104	18.199	40.415	−45.378		118.46	N
ATOM	9375	CA	THR E	104	17.706	39.043	−45.423		121.91	C
ATOM	9376	C	THR E	104	18.453	38.129	−44.461		120.34	C
ATOM	9377	O	THR E	104	18.024	37.003	−44.211		122.09	O
ATOM	9378	CB	THR E	104	17.830	38.452	−46.844		122.12	C
ATOM	9379	OG1	THR E	104	19.214	38.270	−47.169		123.24	O
ATOM	9380	CG2	THR E	104	17.185	39.369	−47.872		125.29	C
ATOM	9381	H	THR E	104	19.052	40.478	−45.288		122.15	H
ATOM	9382	HA	THR E	104	16.768	39.037	−45.176		126.30	H
ATOM	9383	HB	THR E	104	17.377	37.595	−46.875		126.55	H
ATOM	9384	HG1	THR E	104	19.287	37.948	−47.941		127.89	H
ATOM	9385	HG21	THR E	104	17.271	38.985	−48.758		130.35	H
ATOM	9386	HG22	THR E	104	16.244	39.485	−47.668		130.35	H
ATOM	9387	HG23	THR E	104	17.620	40.236	−47.860		130.35	H
ATOM	9388	N	VAL E	105	19.570	38.612	−43.925		123.32	N
ATOM	9389	CA	VAL E	105	20.446	37.784	−43.105		121.10	C
ATOM	9390	C	VAL E	105	20.199	37.994	−41.613		124.91	C
ATOM	9391	O	VAL E	105	20.247	39.116	−41.110		123.61	O
ATOM	9392	CB	VAL E	105	21.928	38.072	−43.414		126.35	C
ATOM	9393	CG1	VAL E	105	22.838	37.197	−42.560		125.25	C
ATOM	9394	CG2	VAL E	105	22.214	37.842	−44.892		128.02	C
ATOM	9395	H	VAL E	105	19.844	39.421	−44.023		127.98	H
ATOM	9396	HA	VAL E	105	20.275	36.850	−43.307		125.32	H
ATOM	9397	HB	VAL E	105	22.121	39.000	−43.210		131.62	H
ATOM	9398	HG11	VAL E	105	23.762	37.400	−42.775		130.30	H
ATOM	9399	HG12	VAL E	105	22.667	37.385	−41.624		130.30	H
ATOM	9400	HG13	VAL E	105	22.649	36.265	−42.751		130.30	H
ATOM	9401	HG21	VAL E	105	23.150	38.028	−45.064		133.63	H
ATOM	9402	HG22	VAL E	105	22.014	36.918	−45.111		133.63	H
ATOM	9403	HG23	VAL E	105	21.655	38.435	−45.417		133.63	H
ATOM	9404	N	LYS E	106	19.944	36.892	−40.916		128.46	N
ATOM	9405	CA	LYS E	106	19.775	36.896	−39.469		132.57	C
ATOM	9406	C	LYS E	106	21.133	36.835	−38.787		131.99	C
ATOM	9407	O	LYS E	106	21.998	36.062	−39.198		130.22	O
ATOM	9408	CB	LYS E	106	18.914	35.706	−39.033		133.52	C
ATOM	9409	CG	LYS E	106	18.726	35.569	−37.528		137.03	C
ATOM	9410	CD	LYS E	106	18.189	34.196	−37.165		145.30	C
ATOM	9411	CE	LYS E	106	17.955	34.067	−35.665		157.12	C
ATOM	9412	NZ	LYS E	106	19.210	34.241	−34.879		154.38	N1+
ATOM	9413	H	LYS E	106	19.862	36.112	−41.269		134.15	H
ATOM	9414	HA	LYS E	106	19.330	37.714	−39.198		139.08	H
ATOM	9415	HB2	LYS E	106	18.035	35.799	−39.431		140.22	H
ATOM	9416	HB3	LYS E	106	19.331	34.890	−39.351		140.22	H
ATOM	9417	HG2	LYS E	106	19.581	35.689	−37.086		144.43	H
ATOM	9418	HG3	LYS E	106	18.092	36.236	−37.222		144.43	H
ATOM	9419	HD2	LYS E	106	17.343	34.054	−37.618		154.35	H
ATOM	9420	HD3	LYS E	106	18.831	33.520	−37.432		154.35	H
ATOM	9421	HE2	LYS E	106	17.325	34.748	−35.382		168.55	H
ATOM	9422	HE3	LYS E	106	17.600	33.184	−35.475		168.55	H
ATOM	9423	HZ1	LYS E	106	19.805	33.622	−35.116		165.26	H
ATOM	9424	HZ2	LYS E	106	19.554	35.047	−35.031		165.26	H
ATOM	9425	HZ3	LYS E	106	19.038	34.159	−34.010		165.26	H
ATOM	9426	N	THR E	107	21.315	37.652	−37.752		130.36	N
ATOM	9427	CA	THR E	107	22.519	37.598	−36.926		139.31	C
ATOM	9428	C	THR E	107	22.178	36.947	−35.588		141.69	C
ATOM	9429	O	THR E	107	21.024	36.604	−35.336		135.99	O
ATOM	9430	CB	THR E	107	23.125	38.998	−36.691		136.74	C
ATOM	9431	OG	THR E	107	22.180	39.833	−36.013		134.87	O
ATOM	9432	CG2	THR E	107	23.513	39.643	−38.017		137.13	C
ATOM	9433	H	THR E	107	20.751	38.253	−37.505		136.43	H
ATOM	9434	HA	THR E	107	23.185	37.050	−37.369		147.17	H
ATOM	9435	HB	THR E	107	23.925	38.913	−36.149		144.09	H
ATOM	9436	HG1	THR E	107	22.509	40.595	−35.885		141.85	H
ATOM	9437	HG21	THR E	107	23.893	40.521	−37.860		144.55	H
ATOM	9438	HG22	THR E	107	24.169	39.093	−38.474		144.55	H
ATOM	9439	HG23	THR E	107	22.730	39.735	−38.582		144.55	H
ATOM	9440	N	GLN E	108	23.180	36.784	−34.731		141.22	N
ATOM	9441	CA	GLN E	108	23.017	36.001	−33.511		151.91	C
ATOM	9442	C	GLN E	108	22.373	36.798	−32.379		144.49	C
ATOM	9443	O	GLN E	108	21.587	36.256	−31.602		143.27	O
ATOM	9444	CB	GLN E	108	24.372	35.461	−33.049		168.26	C
ATOM	9445	CG	GLN E	108	24.287	34.140	−32.303		183.56	C
ATOM	9446	CD	GLN E	108	23.781	33.007	−33.179		191.50	C
ATOM	9447	OE1	GLN E	108	23.967	33.017	−34.397		189.80	O
ATOM	9448	NE2	GLN E	108	23.130	32.028	−32.563		195.77	N
ATOM	9449	H	GLN E	108	23.966	37.116	−34.833		149.46	H
ATOM	9450	HA	GLN E	108	22.444	35.241	−33.701		162.30	H
ATOM	9451	HB2	GLN E	108	24.936	35.327	−33.827		181.91	H
ATOM	9452	HB3	GLN E	108	24.781	36.111	−32.456		181.91	H
ATOM	9453	HG2	GLN E	108	25.171	33.900	−31.982		100.217	H
ATOM	9454	HG3	GLN E	108	23.677	34.238	−31.555		100.217	H
ATOM	9455	HE21	GLN E	108	22.823	31.364	−33.016		114.912	H
ATOM	9456	HE22	GLN E	108	23.014	32.058	−31.711		114.912	H
ATOM	9457	N	GLU E	109	22.717	38.078	−32.288		145.66	N
ATOM	9458	CA	GLU E	109	22.231	38.935	−31.207		142.78	C
ATOM	9459	C	GLU E	109	20.706	39.053	−31.196		140.26	C
ATOM	9460	O	GLU E	109	20.050	38.976	−32.238		131.16	O
ATOM	9461	CB	GLU E	109	22.860	40.332	−31.304		142.62	C
ATOM	9462	CG	GLU E	109	22.975	40.884	−32.724		152.37	C
ATOM	9463	CD	GLU E	109	23.398	42.343	−32.764		159.49	C
ATOM	9464	OE1	GLU E	109	23.528	42.964	−31.686		162.06	O
ATOM	9465	OE2	GLU E	109	23.602	42.868	−33.881		151.48	O1−
ATOM	9466	H	GLU E	109	23.234	38.481	−32.845		154.80	H
ATOM	9467	HA	GLU E	109	22.502	38.548	−30.359		151.33	H
ATOM	9468	HB2	GLU E	109	22.317	40.952	−30.791		151.15	H
ATOM	9469	HB3	GLU E	109	23.754	40.296	−30.929		151.15	H
ATOM	9470	HG2	GLU E	109	23.638	40.367	−33.209		162.84	H
ATOM	9471	HG3	GLU E	109	22.113	40.810	−33.161		162.84	H
ATOM	9472	N	ALA E	110	20.150	39.233	−30.001		141.90	N
ATOM	9473	CA	ALA E	110	18.712	39.410	−29.837		133.67	C
ATOM	9474	C	ALA E	110	18.339	40.867	−30.069		135.94	C
ATOM	9475	O	ALA E	110	18.587	41.730	−29.225		134.30	O
ATOM	9476	CB	ALA E	110	18.270	38.958	−28.455		141.21	C
ATOM	9477	H	ALA E	110	20.590	39.258	−29.263		150.29	H
ATOM	9478	HA	ALA E	110	18.247	38.869	−30.495		140.41	H
ATOM	9479	HB1	ALA E	110	17.312	39.086	−28.372		149.45	H
ATOM	9480	HB2	ALA E	110	18.490	38.020	−28.344		149.45	H
ATOM	9481	HB3	ALA E	110	18.734	39.488	−27.787		149.45	H
ATOM	9482	N	THR E	111	17.745	41.129	−31.226		123.46	N
ATOM	9483	CA	THR E	111	17.372	42.476	−31.620		123.33	C
ATOM	9484	C	THR E	111	15.999	42.480	−32.272		119.12	C
ATOM	9485	O	THR E	111	15.517	41.447	−32.737		117.50	O
ATOM	9486	CB	THR E	111	18.375	43.062	−32.609		121.03	C
ATOM	9487	OG1	THR E	111	18.395	42.245	−33.786		119.06	O
ATOM	9488	CG2	THR E	111	19.769	43.117	−31.995		130.25	C
ATOM	9489	H	THR E	111	17.546	40.530	−31.811		128.16	H
ATOM	9490	HA	THR E	111	17.342	43.047	−30.837		128.00	H
ATOM	9491	HB	THR E	111	18.107	43.963	−32.846		125.24	H
ATOM	9492	HG1	THR E	111	18.944	42.555	−34.341		122.88	H
ATOM	9493	HG21	THR E	111	20.397	43.491	−32.633		136.30	H
ATOM	9494	HG22	THR E	111	19.759	43.673	−31.200		136.30	H
ATOM	9495	HG23	THR E	111	20.060	42.225	−31.753		136.30	H
ATOM	9496	N	ASN E	112	15.383	43.653	−32.322		118.03	N
ATOM	9497	CA	ASN E	112	14.118	43.813	−33.014		118.86	C
ATOM	9498	C	ASN E	112	14.283	43.492	−34.496		118.90	C
ATOM	9499	O	ASN E	112	13.396	42.909	−35.116		115.74	O
ATOM	9500	CB	ASN E	112	13.581	45.231	−32.820		119.71	C
ATOM	9501	CG	ASN E	112	13.143	45.494	−31.389		124.98	C
ATOM	9502	OD1	ASN E	112	12.646	44.597	−30.710		122.68	O
ATOM	9503	ND2	ASN E	112	13.331	46.723	−30.923		122.07	N
ATOM	9504	H	ASN E	112	15.680	44.375	−31.960		121.63	H
ATOM	9505	HA	ASN E	112	13.472	43.192	−32.642		122.63	H
ATOM	9506	HB2	ASN E	112	14.278	45.867	−33.044		123.65	H
ATOM	9507	HB3	ASN E	112	12.813	45.361	−33.399		123.65	H
ATOM	9508	HD21	ASN E	112	13.098	46.918	−30.118		126.49	H
ATOM	9509	HD22	ASN E	112	13.684	47.325	−31.426		126.49	H
ATOM	9510	N	LYS E	113	15.439	43.854	−35.047		116.41	N
ATOM	9511	CA	LYS E	113	15.739	43.600	−36.451		115.65	C
ATOM	9512	C	LYS E	113	15.712	42.103	−36.766		116.82	C
ATOM	9513	O	LYS E	113	15.106	41.673	−37.751		116.67	O
ATOM	9514	CB	LYS E	113	17.102	44.193	−36.806		120.54	C
ATOM	9515	CG	LYS E	113	17.454	44.125	−38.276		120.47	C
ATOM	9516	CD	LYS E	113	18.816	44.753	−38.539		122.73	C
ATOM	9517	CE	LYS E	113	19.154	44.754	−40.019		124.48	C
ATOM	9518	NZ	LYS E	113	20.513	45.300	−40.281		126.06	N1+
ATOM	9519	H	LYS E	113	16.072	44.253	−34.623		119.69	H
ATOM	9520	HA	LYS E	113	15.069	44.035	−37.002		118.78	H
ATOM	9521	HB2	LYS E	113	17.112	45.127	−36.544		124.65	H
ATOM	9522	HB3	LYS E	113	17.787	43.710	−36.317		124.65	H
ATOM	9523	HG2	LYS E	113	17.486	43.197	−38.557		124.56	H
ATOM	9524	HG3	LYS E	113	16.789	44.611	−38.789		124.56	H
ATOM	9525	HD2	LYS E	113	18.809	45.672	−38.228		127.28	H
ATOM	9526	HD3	LYS E	113	19.497	44.246	−38.071		127.28	H
ATOM	9527	HE2	LYS E	113	19.125	43.844	−40.352		129.38	H
ATOM	9528	HE3	LYS E	113	18.511	45.305	−40.492		129.38	H
ATOM	9529	HZ1	LYS E	113	20.565	46.139	−39.988		131.27	H
ATOM	9530	HZ2	LYS E	113	21.124	44.808	−39.861		131.27	H
ATOM	9531	HZ3	LYS E	113	20.682	45.288	−41.155		131.27	H
ATOM	9532	N	ASN E	114	16.360	41.307	−35.924		114.24	N
ATOM	9533	CA	ASN E	114	16.389	39.862	−36.127		115.14	C
ATOM	9534	C	ASN E	114	15.036	39.200	−35.892		113.48	C
ATOM	9535	O	ASN E	114	14.623	38.335	−36.663		114.71	O
ATOM	9536	CB	ASN E	114	17.440	39.224	−35.217		120.17	C
ATOM	9537	CG	ASN E	114	18.851	39.385	−35.758		127.46	C
ATOM	9538	OD1	ASN E	114	19.069	39.370	−36.971		122.82	O
ATOM	9539	ND2	ASN E	114	19.815	39.537	−34.858		124.63	N
ATOM	9540	H	ASN E	114	16.790	41.576	−35.230		117.09	H
ATOM	9541	HA	ASN E	114	16.648	39.684	−37.045		118.17	H
ATOM	9542	HB2	ASN E	114	17.402	39.647	−34.345		124.21	H
ATOM	9543	HB3	ASN E	114	17.255	38.276	−35.136		124.21	H
ATOM	9544	HD21	ASN E	114	20.631	39.631	−35.114		129.56	H
ATOM	9545	HD22	ASN E	114	19.624	39.540	−34.019		129.56	H
ATOM	9546	N	MET E	115	14.350	39.596	−34.827		114.19	N
ATOM	9547	CA	MET E	115	13.049	39.018	−34.518		115.83	C
ATOM	9548	C	MET E	115	12.046	39.333	−35.625		115.36	C
ATOM	9549	O	MET E	115	11.231	38.490	−36.006		114.90	O
ATOM	9550	CB	MET E	115	12.536	39.543	−33.179		117.26	C
ATOM	9551	CG	MET E	115	11.267	38.858	−32.708		123.77	C
ATOM	9552	SD	MET E	115	10.596	39.578	−31.197		135.74	S
ATOM	9553	CE	MET E	115	11.976	39.355	−30.071		145.72	C
ATOM	9554	I	MET E	115	14.614	40.195	−34.270		117.03	H
ATOM	9555	HA	MET E	115	13.142	38.056	−34.444		119.00	H
ATOM	9556	HB2	MET E	115	13.218	39.402	−32.505		120.71	H
ATOM	9557	HB3	MET E	115	12.348	40.491	−33.265		120.71	H
ATOM	9558	HG2	MET E	115	10.592	38.933	−33.400		128.52	H
ATOM	9559	HG3	MET E	115	11.460	37.923	−32.533		128.52	H
ATOM	9560	HE1	MET E	115	11.735	39.711	−29.202		154.87	H
ATOM	9561	HE2	MET E	115	12.173	38.408	−29.998		154.87	H
ATOM	9562	HE3	MET E	115	12.748	39.828	−30.420		154.87	H
ATOM	9563	N	TRP E	116	12.109	40.558	−36.130		112.48	N
ATOM	9564	CA	TRP E	116	11.240	40.990	−37.216		115.47	C
ATOM	9565	C	TRP E	116	11.452	40.113	−38.447		114.04	C
ATOM	9566	O	TRP E	116	10.498	39.712	−39.112		111.48	O
ATOM	9567	CB	TRP E	116	11.515	42.458	−37.544		112.64	C
ATOM	9568	CG	TRP E	116	10.633	43.043	−38.607		112.35	C
ATOM	9569	CD1	TRP E	116	10.933	43.189	−39.929		112.04	C
ATOM	9570	CD2	TRP E	116	9.312	43.572	−38.435		114.43	C
ATOM	9571	NE1	TRP E	116	9.883	43.779	−40.593		114.64	N
ATOM	9572	CE2	TRP E	116	8.874	44.021	−39.699		113.81	C
ATOM	9573	CE3	TRP E	116	8.459	43.711	−37.336		111.41	C
ATOM	9574	CZ2	TRP E	116	7.624	44.603	−39.892		114.26	C
ATOM	9575	CZ3	TRP E	116	7.216	44.288	−37.531		115.87	C
ATOM	9576	CH2	TRP E	116	6.811	44.726	−38.799		114.11	C
ATOM	9577	H	TRP E	116	12.653	41.165	−35.857		114.98	H
ATOM	9578	HA	TRP E	116	10.314	40.907	−36.938		118.56	H
ATOM	9579	HB2	TRP E	116	11.390	42.983	−36.738		115.17	H
ATOM	9580	HB3	TRP E	116	12.432	42.540	−37.847		115.17	H
ATOM	9581	HD1	TRP E	116	11.734	42.930	−40.324		114.44	H
ATOM	9582	HE1	TRP E	116	9.862	43.961	−41.433		117.57	H
ATOM	9583	HE3	TRP E	116	8.723	43.427	−36.491		113.69	H
ATOM	9584	HZ2	TRP E	116	7.351	44.891	−40.733		117.11	H
ATOM	9585	HZ3	TRP E	116	6.639	44.385	−36.808		119.05	H
ATOM	9586	HH2	TRP E	116	5.967	45.105	−38.901		116.94	H
ATOM	9587	N	LEU E	117	12.714	39.810	−38.725		113.03	N
ATOM	9588	CA	LEU E	117	13.093	39.003	−39.878		113.36	C
ATOM	9589	C	LEU E	117	12.619	37.564	−39.748		115.88	C
ATOM	9590	O	LEU E	117	12.149	36.968	−40.719		115.15	O
ATOM	9591	CB	LEU E	117	14.618	39.027	−40.063		113.94	C
ATOM	9592	CG	LEU E	117	15.204	38.145	−41.175		115.98	C
ATOM	9593	CD1	LEU E	117	14.745	38.606	−42.552		116.70	C
ATOM	9594	CD2	LEU E	117	16.725	38.130	−41.103		124.05	C
ATOM	9595	H	LEU E	117	13.384	40.067	−38.251		115.63	H
ATOM	9596	HA	LEU E	117	12.688	39.381	−40.674		116.03	H
ATOM	9597	HB2	LEU E	117	14.884	39.940	−40.254		116.73	H
ATOM	9598	HB3	LEU E	117	15.027	38.744	−39.230		116.73	H
ATOM	9599	HG	LEU E	117	14.892	37.235	−41.048		119.17	H
ATOM	9600	HD11	LEU E	117	15.135	38.026	−43.225		120.03	H
ATOM	9601	HD12	LEU E	117	13.777	38.559	−42.594		120.03	H
ATOM	9602	HD13	LEU E	117	15.039	39.520	−42.693		120.03	H
ATOM	9603	HD21	LEU E	117	17.069	37.567	−41.814		128.86	H
ATOM	9604	HD22	LEU E	117	17.055	39.036	−41.209		128.86	H
ATOM	9605	HD23	LEU E	117	16.997	37.777	−40.241		128.86	H
ATOM	9606	N	THR E	118	12.748	37.002	−38.552		111.16	N
ATOM	9607	CA	THR E	118	12.450	35.592	−38.362		115.63	C
ATOM	9608	C	THR E	118	10.994	35.308	−37.997		115.23	C
ATOM	9609	O	THR E	118	10.612	34.141	−37.919		116.44	O
ATOM	9610	CB	THR E	118	13.340	34.974	−37.268		117.43	C
ATOM	9611	OG1	THR E	118	13.079	35.606	−36.008		119.94	O
ATOM	9612	CG2	THR E	118	14.807	35.139	−37.623		121.12	C
ATOM	9613	H	THR E	118	13.004	37.412	−37.840		113.39	H
ATOM	9614	HA	THR E	118	12.639	35.124	−39.190		118.76	H
ATOM	9615	HB	THR E	118	13.149	34.026	−37.197		120.92	H
ATOM	9616	HG1	THR E	118	12.273	35.500	−35.795		123.93	H
ATOM	9617	HG21	THR E	118	15.362	34.748	−36.930		125.34	H
ATOM	9618	HG22	THR E	118	14.996	34.697	−38.465		125.34	H
ATOM	9619	HG23	THR E	118	15.024	36.081	−37.707		125.34	H
ATOM	9620	N	THR E	119	10.183	36.346	−37.781		113.58	N
ATOM	9621	CA	THR E	119	8.800	36.131	−37.326		112.81	C
ATOM	9622	C	THR E	119	7.709	36.798	−38.158		115.49	C
ATOM	9623	O	THR E	119	6.530	36.502	−37.968		114.16	O
ATOM	9624	CB	THR E	119	8.595	36.627	−35.875		112.82	C
ATOM	9625	OG1	THR E	119	8.665	38.059	−35.835		112.89	O
ATOM	9626	CG2	THR E	119	9.626	36.020	−34.943		117.46	C
ATOM	9627	H	THR E	119	10.401	37.171	−37.886		116.30	H
ATOM	9628	HA	THR E	119	8.624	35.177	−37.333		115.37	H
ATOM	9629	HB	THR E	119	7.717	36.348	−35.570		115.38	H
ATOM	9630	HG1	THR E	119	9.416	38.318	−36.110		115.47	H
ATOM	9631	HG21	THR E	119	9.484	36.341	−34.038		120.95	H
ATOM	9632	HG22	THR E	119	9.551	35.053	−34.950		120.95	H
ATOM	9633	HG23	THR E	119	10.518	36.270	−35.229		120.95	H
ATOM	9634	N	SER E	120	8.075	37.705	−39.056		111.68	N
ATOM	9635	CA	SER E	120	7.067	38.444	−39.814		115.43	C
ATOM	9636	C	SER E	120	6.196	37.531	−40.684		112.04	C
ATOM	9637	O	SER E	120	4.966	37.593	−40.619		110.68	O
ATOM	9638	CB	SER E	120	7.737	39.510	−40.682		114.31	C
ATOM	9639	OG	SER E	120	8.074	40.644	−39.901		113.97	O
ATOM	9640	H	SER E	120	8.888	37.911	−39.244		114.01	H
ATOM	9641	HA	SER E	120	6.482	38.899	−39.189		118.51	H
ATOM	9642	HB2	SER E	120	8.546	39.140	−41.070		117.18	H
ATOM	9643	HB3	SER E	120	7.124	39.778	−41.384		117.18	H
ATOM	9644	HG	SER E	120	8.604	40.424	−39.288		116.76	H
ATOM	9645	N	GLU E	121	6.827	36.691	−41.502		113.53	N
ATOM	9646	CA	GLU E	121	6.080	35.770	−42.357		116.10	C
ATOM	9647	C	GLU E	121	5.202	34.861	−41.501		114.09	C
ATOM	9648	O	GLU E	121	4.025	34.658	−41.788		114.66	O
ATOM	9649	CB	GLU E	121	7.030	34.933	−43.222		118.39	C
ATOM	9650	CG	GLU E	121	6.315	34.029	−44.220		117.83	C
ATOM	9651	CD	GLU E	121	7.270	33.236	−45.097		126.57	C
ATOM	9652	OE1	GLU E	121	8.499	33.395	−44.946		129.79	O
ATOM	9653	OE2	GLU E	121	6.786	32.450	−45.940		128.08	O1−
ATOM	9654	H	GLU E	121	7.681	36.635	−41.580		116.24	H
ATOM	9655	HA	GLU E	121	5.503	36.279	−42.947		119.32	H
ATOM	9656	HB2	GLU E	121	7.606	35.532	−43.723		122.07	H
ATOM	9657	HB3	GLU E	121	7.566	34.370	−42.642		122.07	H
ATOM	9658	HG2	GLU E	121	5.761	33.399	−43.734		121.40	H
ATOM	9659	HG3	GLU E	121	5.762	34.576	−44.800		121.40	H
ATOM	9660	N	PHE E	122	5.798	34.331	−40.439		113.77	N
ATOM	9661	CA	PHE E	122	5.101	33.510	−39.458		114.62	C
ATOM	9662	C	PHE E	122	3.851	34.212	−38.924		114.41	C
ATOM	9663	O	PHE E	122	2.760	33.641	−38.928		113.91	O
ATOM	9664	CB	PHE E	122	6.072	33.171	−38.319		116.68	C
ATOM	9665	CG	PHE E	122	5.445	32.476	−37.144		116.24	C
ATOM	9666	CD1	PHE E	122	5.386	31.093	−37.091		119.07	C
ATOM	9667	CD2	PHE E	122	4.959	33.204	−36.070		117.52	C
ATOM	9668	CE1	PHE E	122	4.830	30.451	−36.003		120.81	C
ATOM	9669	CE2	PHE E	122	4.398	32.568	−34.980		121.23	C
ATOM	9670	CZ	PHE E	122	4.337	31.189	−34.944		122.10	C
ATOM	9671	H	PHE E	122	6.633	34.438	−40.261		116.53	H
ATOM	9672	HA	PHE E	122	4.825	32.680	−39.877		117.54	H
ATOM	9673	HB2	PHE E	122	6.766	32.589	−38.667		120.02	H
ATOM	9674	HB3	PHE E	122	6.469	33.994	−37.995		120.02	H
ATOM	9675	HD1	PHE E	122	5.717	30.591	−37.801		122.89	H
ATOM	9676	HD2	PHE E	122	4.998	34.133	−36.089		121.02	H
ATOM	9677	HE1	PHE E	122	4.787	29.522	−35.983		124.98	H
ATOM	9678	HE2	PHE E	122	4.067	33.068	−34.268		125.48	H
ATOM	9679	HZ	PHE E	122	3.959	30.758	−34.211		126.52	H
ATOM	9680	N	ARG E	123	4.008	35.459	−38.491		19.96	N
ATOM	9681	CA	ARG E	123	2.915	36.190	−37.862		112.21	C
ATOM	9682	C	ARG E	123	1.821	36.555	−38.871		113.20	C
ATOM	9683	O	ARG E	123	0.660	36.720	−38.501		116.26	O
ATOM	9684	CB	ARG E	123	3.461	37.442	−37.164		113.63	C
ATOM	9685	CG	ARG E	123	4.080	37.153	−35.797		114.82	C
ATOM	9686	CD	ARG E	123	5.182	38.138	−35.440		119.31	C
ATOM	9687	NE	ARG E	123	4.809	39.485	−35.833		125.00	N
ATOM	9688	CZ	ARG E	123	5.551	40.304	−36.569		113.96	C
ATOM	9689	NH1	ARG E	123	6.763	39.963	−36.994		117.77	N1+
ATOM	9690	NH2	ARG E	123	5.076	41.500	−36.857		120.81	N
ATOM	9691	H	ARG E	123	4.741	35.905	−38.551		111.95	H
ATOM	9692	HA	ARG E	123	2.513	35.625	−37.183		114.65	H
ATOM	9693	HB2	ARG E	123	4.147	37.839	−37.724		116.36	H
ATOM	9694	HB3	ARG E	123	2.735	38.072	−37.035		116.36	H
ATOM	9695	HG2	ARG E	123	3.391	37.212	−35.117		117.78	H
ATOM	9696	HG3	ARG E	123	4.464	36.262	−35.805		117.78	H
ATOM	9697	HD2	ARG E	123	5.326	38.127	−34.481		123.17	H
ATOM	9698	HD3	ARG E	123	5.996	37.896	−35.908		123.17	H
ATOM	9699	HE	ARG E	123	4.045	39.776	−35.567		130.00	H
ATOM	9700	HH11	ARG E	123	7.080	39.185	−36.811		121.33	H
ATOM	9701	HH12	ARG E	123	7.225	40.516	−37.464		121.33	H
ATOM	9702	HH21	ARG E	123	4.296	41.732	−36.579		124.98	H
ATOM	9703	HH22	ARG E	123	5.547	42.049	−37.323		124.98	H
ATOM	9704	N	LEU E	124	2.184	36.657	−40.146		111.77	N
ATOM	9705	CA	LEU E	124	1.207	36.917	−41.200		112.92	C
ATOM	9706	C	LEU E	124	0.445	35.654	−41.598		114.87	C
ATOM	9707	O	LEU E	124	−0.771	35.691	−41.805		114.46	O
ATOM	9708	CB	LEU E	124	1.890	37.508	−42.437		114.80	C
ATOM	9709	CG	LEU E	124	1.021	37.592	−43.700		111.83	C
ATOM	9710	CD1	LEU E	124	−0.216	38.439	−43.460		115.58	C
ATOM	9711	CD2	LEU E	124	1.822	38.135	−44.871		114.19	C
ATOM	9712	H	LEU E	124	2.993	36.579	−40.429		114.12	H
ATOM	9713	HA	LEU E	124	0.561	37.565	−40.877		115.50	H
ATOM	9714	HB2	LEU E	124	2.182	38.408	−42.225		117.76	H
ATOM	9715	HB3	LEU E	124	2.661	36.961	−42.652		117.76	H
ATOM	9716	HG	LEU E	124	0.725	36.698	−43.934		114.19	H
ATOM	9717	HD11	LEU E	124	−0.740	38.470	−44.276		118.69	H
ATOM	9718	HD12	LEU E	124	−0.738	38.040	−42.746		118.69	H
ATOM	9719	HD13	LEU E	124	0.059	39.335	−43.209		118.69	H
ATOM	9720	HD21	LEU E	124	1.250	38.177	−45.652		117.03	H
ATOM	9721	HD22	LEU E	124	2.144	39.022	−44.648		117.03	H
ATOM	9722	HD23	LEU E	124	2.572	37.544	−45.041		117.03	H
ATOM	9723	N	LYS E	125	1.158	34.538	−41.705		113.01	N
ATOM	9724	CA	LYS E	125	0.593	33.347	−42.336		115.82	C
ATOM	9725	C	LYS E	125	−0.148	32.421	−41.379		117.64	C
ATOM	9726	O	LYS E	125	−0.543	31.320	−41.758		113.71	O
ATOM	9727	CB	LYS E	125	1.698	32.572	−43.050		113.96	C
ATOM	9728	CG	LYS E	125	2.202	33.285	−44.298		120.01	C
ATOM	9729	CD	LYS E	125	3.130	32.408	−45.114		123.78	C
ATOM	9730	CE	LYS E	125	3.436	33.035	−46.467		122.29	C
ATOM	9731	NZ	LYS E	125	4.222	32.110	−47.321		126.85	N1+
ATOM	9732	H	LYS E	125	1.965	34.443	−41.424		115.61	H
ATOM	9733	HA	LYS E	125	−0.043	33.633	−43.010		118.98	H
ATOM	9734	HB2	LYS E	125	2.448	32.461	−42.444		116.76	H
ATOM	9735	HB3	LYS E	125	1.355	31.705	−43.317		116.76	H
ATOM	9736	HG2	LYS E	125	1.446	33.526	−44.855		124.01	H
ATOM	9737	HG3	LYS E	125	2.691	34.080	−44.035		124.01	H
ATOM	9738	HD2	LYS E	125	3.965	32.292	−44.635		128.53	H
ATOM	9739	HD3	LYS E	125	2.707	31.548	−45.265		128.53	H
ATOM	9740	HE2	LYS E	125	2.604	33.238	−46.922		126.74	H
ATOM	9741	HE3	LYS E	125	3.955	33.844	−46.335		126.74	H
ATOM	9742	HZ1	LYS E	125	4.392	32.492	−48.106		132.22	H
ATOM	9743	HZ2	LYS E	125	4.993	31.910	−46.923		132.22	H
ATOM	9744	HZ3	LYS E	125	3.764	31.359	−47.457		132.22	H
ATOM	9745	N	LYS E	126	−0.352	32.867	−40.145		115.49	N
ATOM	9746	CA	LYS E	126	−1.062	32.056	−39.168		114.17	C
ATOM	9747	C	LYS E	126	−2.423	31.628	−39.718		114.30	C
ATOM	9748	O	LYS E	126	−2.765	30.447	−39.682		114.19	O
ATOM	9749	CB	LYS E	126	−1.230	32.826	−37.862		113.34	C
ATOM	9750	CG	LYS E	126	−1.750	31.990	−36.705		116.84	C
ATOM	9751	CD	LYS E	126	−1.636	32.761	−35.400		120.30	C
ATOM	9752	CE	LYS E	126	−2.149	31.960	−34.218		123.97	C
ATOM	9753	NZ	LYS E	126	−1.883	32.674	−32.933		126.21	N1+
ATOM	9754	H	LYS E	126	−0.091	33.632	−39.851		118.59	H
ATOM	9755	HA	LYS E	126	−0.546	31.257	−38.983		117.00	H
ATOM	9756	HB2	LYS E	126	−0.368	33.187	−37.601		116.00	H
ATOM	9757	HB3	LYS E	126	−1.858	33.551	−38.007		116.00	H
ATOM	9758	HG2	LYS E	126	−2.684	31.775	−36.855		120.21	H
ATOM	9759	HG3	LYS E	126	−1.223	31.179	−36.630		120.21	H
ATOM	9760	HD2	LYS E	126	−0.704	32.977	−35.238		124.36	H
ATOM	9761	HD3	LYS E	126	−2.161	33.575	−35.464		124.36	H
ATOM	9762	HE2	LYS E	126	−3.106	31.835	−34.305		128.76	H
ATOM	9763	HE3	LYS E	126	−1.697	31.103	−34.190		128.76	H
ATOM	9764	HZ1	LYS E	126	−1.008	32.800	−32.830		131.45	H
ATOM	9765	HZ2	LYS E	126	−2.290	33.466	−32.935		131.45	H
ATOM	9766	HZ3	LYS E	126	−2.188	32.193	−32.249		131.45	H
ATOM	9767	N	TRP E	127	−3.177	32.587	−40.254		113.47	N
ATOM	9768	CA	TRP E	127	−4.497	32.314	−40.828		113.36	C
ATOM	9769	C	TRP E	127	−4.575	32.682	−42.311		114.64	C
ATOM	9770	O	TRP E	127	−5.632	32.557	−42.929		113.48	O
ATOM	9771	CB	TRP E	127	−5.573	33.078	−40.053		113.26	C
ATOM	9772	CG	TRP E	127	−5.758	32.580	−38.653		116.00	C
ATOM	9773	CD1	TRP E	127	−5.306	33.163	−37.508		116.46	C
ATOM	9774	CD2	TRP E	127	−6.437	31.386	−38.256		114.01	C
ATOM	9775	NE1	TRP E	127	−5.666	32.408	−36.419		120.27	N
ATOM	9776	CE2	TRP E	127	−6.365	31.312	−36.851		119.93	C
ATOM	9777	CE3	TRP E	127	−7.108	30.374	−38.951		120.52	C
ATOM	9778	CZ2	TRP E	127	−6.931	30.266	−36.129		117.91	C
ATOM	9779	CZ3	TRP E	127	−7.672	29.339	−38.232		122.57	C
ATOM	9780	CH2	TRP E	127	−7.579	29.291	−36.835		125.03	C
ATOM	9781	H	TRP E	127	−2.944	33.413	−40.298		116.16	H
ATOM	9782	HA	TRP E	127	−4.686	31.367	−40.745		116.03	H
ATOM	9783	HB2	TRP E	127	−5.322	34.014	−40.006		115.92	H
ATOM	9784	HB3	TRP E	127	−6.420	32.986	−40.517		115.92	H
ATOM	9785	HD1	TRP E	127	−4.823	33.957	−37.470		119.75	H
ATOM	9786	HE1	TRP E	127	−5.484	32.594	−35.599		124.32	H
ATOM	9787	HE3	TRP E	127	−7.174	30.400	−39.878		124.62	H
ATOM	9788	HZ2	TRP E	127	−6.873	30.232	−35.201		121.50	H
ATOM	9789	HZ3	TRP E	127	−8.119	28.660	−38.684		127.09	H
ATOM	9790	HH2	TRP E	127	−7.969	28.581	−36.378		130.03	H
ATOM	9791	N	PHE E	128	−3.452	33.118	−42.876		113.43	N
ATOM	9792	CA	PHE E	128	−3.425	33.694	−44.221		112.84	C
ATOM	9793	C	PHE E	128	−2.168	33.275	−44.986		114.69	C
ATOM	9794	O	PHE E	128	−1.174	33.999	−44.999		114.50	O
ATOM	9795	CB	PHE E	128	−3.509	35.223	−44.122		115.03	C
ATOM	9796	CG	PHE E	128	−3.640	35.922	−45.446		115.62	C
ATOM	9797	CD1	PHE E	128	−4.757	35.729	−46.242		114.48	C
ATOM	9798	CD2	PHE E	128	−2.660	36.800	−45.879		117.09	C
ATOM	9799	CE1	PHE E	128	−4.884	36.381	−47.456		114.50	C
ATOM	9800	CE2	PHE E	128	−2.780	37.454	−47.092		118.86	C
ATOM	9801	CZ	PHE E	128	−3.895	37.245	−47.881		119.29	C
ATOM	9802	H	PHE E	128	−2.680	33.091	−42.497		116.11	H
ATOM	9803	HA	PHE E	128	−4.198	33.381	−44.717		115.40	H
ATOM	9804	HB2	PHE E	128	−4.283	35.457	−43.587		118.04	H
ATOM	9805	HB3	PHE E	128	−2.703	35.551	−43.694		118.04	H
ATOM	9806	HD1	PHE E	128	−5.426	35.147	−45.961		117.38	H
ATOM	9807	HD2	PHE E	128	−1.906	36.942	−45.353		120.50	H
ATOM	9808	HE1	PHE E	128	−5.636	36.239	−47.985		117.40	H
ATOM	9809	HE2	PHE E	128	−2.112	38.036	−47.376		122.63	H
ATOM	9810	HZ	PHE E	128	−3.979	37.684	−48.696		123.15	H
ATOM	9811	N	ASP E	129	−2.214	32.108	−45.627		114.98	N
ATOM	9812	CA	ASP E	129	−1.055	31.599	−46.357		114.76	C
ATOM	9813	C	ASP E	129	−1.064	32.076	−47.809		117.71	C
ATOM	9814	O	ASP E	129	−1.931	32.851	−48.215		115.50	O
ATOM	9815	CB	ASP E	129	−0.998	30.064	−46.290		114.79	C
ATOM	9816	CG	ASP E	129	−2.224	29.383	−46.902		119.45	C
ATOM	9817	OD1	ASP E	129	−2.824	29.921	−47.858		114.89	O
ATOM	9818	OD2	ASP E	129	−2.571	28.277	−46.430		117.87	O1−
ATOM	9819	H	ASP E	129	−2.903	31.593	−45.653		117.98	H
ATOM	9820	HA	ASP E	129	−0.250	31.942	−45.939		117.72	H
ATOM	9821	HB2	ASP E	129	−0.215	29.757	−46.773		117.74	H
ATOM	9822	HB3	ASP E	129	−0.940	29.792	−45.361		117.74	H
ATOM	9823	N	GLY E	130	−0.093	31.611	−48.587		115.51	N
ATOM	9824	CA	GLY E	130	0.049	32.047	−49.964		115.30	C
ATOM	9825	C	GLY E	130	−1.162	31.724	−50.821		117.27	C
ATOM	9826	O	GLY E	130	−1.603	32.546	−51.628		113.78	O
ATOM	9827	H	GLY E	130	0.499	31.040	−48.337		118.61	H
ATOM	9828	HA2	GLY E	130	0.188	33.007	−49.984		118.37	H
ATOM	9829	HA3	GLY E	130	0.824	31.618	−50.358		118.37	H
ATOM	9830	N	GLU E	131	−1.702	30.522	−50.651		111.94	N
ATOM	9831	CA	GLU E	131	−2.873	30.109	−51.409		116.34	C
ATOM	9832	C	GLU E	131	−4.066	31.011	−51.092		117.14	C
ATOM	9833	O	GLU E	131	−4.838	31.359	−51.984		115.64	O
ATOM	9834	CB	GLU E	131	−3.210	28.648	−51.121		118.79	C
ATOM	9835	CG	GLU E	131	−4.237	28.065	−52.074		125.42	C
ATOM	9836	CD	GLU E	131	−4.437	26.574	−51.886		125.71	C
ATOM	9837	OE1	GLU E	131	−3.919	26.017	−50.892		123.82	O
ATOM	9838	OE2	GLU E	131	−5.110	25.960	−52.743		128.51	O1−
ATOM	9839	H	GLU E	131	−1.409	29.929	−50.101		114.32	H
ATOM	9840	HA	GLU E	131	−2.680	30.190	−52.357		119.61	H
ATOM	9841	HB2	GLU E	131	−2.401	28.118	−51.195		122.54	H
ATOM	9842	HB3	GLU E	131	−3.567	28.580	−50.221		122.54	H
ATOM	9843	HG2	GLU E	131	−5.090	28.503	−51.925		130.51	H
ATOM	9844	HG3	GLU E	131	−3.942	28.215	−52.986		130.51	H
ATOM	9845	N	ASP E	132	−4.207	31.390	−49.824		114.43	N
ATOM	9846	CA	ASP E	132	−5.244	32.334	−49.421		116.97	C
ATOM	9847	C	ASP E	132	−5.081	33.673	−50.140		115.70	C
ATOM	9848	O	ASP E	132	−6.053	34.244	−50.630		113.91	O
ATOM	9849	CB	ASP E	132	−5.220	32.562	−47.904		115.21	C
ATOM	9850	CG	ASP E	132	−5.483	31.294	−47.113		117.73	C
ATOM	9851	OD1	ASP E	132	−6.201	30.405	−47.621		116.20	O
ATOM	9852	OD2	ASP E	132	−4.974	31.192	−45.972		115.44	O1−
ATOM	9853	H	ASP E	132	−3.713	31.114	−49.176		117.31	H
ATOM	9854	HA	ASP E	132	−6.112	31.971	−49.656		120.37	H
ATOM	9855	HB2	ASP E	132	−4.346	32.898	−47.649		118.25	H
ATOM	9856	HB3	ASP E	132	−5.905	33.208	−47.671		118.25	H
ATOM	9857	N	CYS E	133	−3.849	34.168	−50.198		112.86	N
ATOM	9858	CA	CYS E	133	−3.571	35.454	−50.826		112.73	C
ATOM	9859	C	CYS E	133	−3.981	35.443	−52.295		114.86	C
ATOM	9860	O	CYS E	133	−4.539	36.417	−52.798		115.23	O
ATOM	9861	CB	CYS E	133	−2.086	35.805	−50.691		121.39	C
ATOM	9862	SG	CYS E	133	−1.610	37.374	−51.458		123.37	S
ATOM	9863	H	CYS E	133	−3.153	33.776	−49.880		115.43	H
ATOM	9864	HA	CYS E	133	−4.084	36.143	−50.376		115.28	H
ATOM	9865	HB2	CYS E	133	−1.864	35.860	−49.749		125.67	H
ATOM	9866	HB3	CYS E	133	−1.562	35.103	−51.109		125.67	H
ATOM	9867	N	ILE E	134	−3.718	34.331	−52.974		113.95	N
ATOM	9868	CA	ILE E	134	−4.075	34.191	−54.382		113.37	C
ATOM	9869	C	ILE E	134	−5.593	34.152	−54.551		114.47	C
ATOM	9870	O	ILE E	134	−6.141	34.750	−55.476		112.81	O
ATOM	9871	CB	ILE E	134	−3.457	32.910	−54.996		118.31	C
ATOM	9872	CG1	ILE E	134	−1.924	32.990	−54.988		113.13	C
ATOM	9873	CG2	ILE E	134	−3.982	32.670	−56.416		119.91	C
ATOM	9874	CD1	ILE E	134	−1.336	34.002	−55.955		113.23	C
ATOM	9875	H	ILE E	134	−3.332	33.639	−52.641		116.74	H
ATOM	9876	HA	ILE E	134	−3.735	34.955	−54.873		116.04	H
ATOM	9877	HB	ILE E	134	−3.721	32.156	−54.447		121.97	H
ATOM	9878	HG12	ILE E	134	−1.632	33.232	−54.096		115.76	H
ATOM	9879	HG13	ILE E	134	−1.568	32.118	−55.222		115.76	H
ATOM	9880	HG21	ILE E	134	−3.576	31.863	−56.770		123.89	H
ATOM	9881	HG22	ILE E	134	−4.946	32.569	−56.382		123.89	H
ATOM	9882	HG23	ILE E	134	−3.748	33.430	−56.971		123.89	H
ATOM	9883	HD11	ILE E	134	−0.369	33.983	−55.881		115.87	H
ATOM	9884	HD12	ILE E	134	−1.604	33.769	−56.858		115.87	H
ATOM	9885	HD13	ILE E	134	−1.668	34.885	−55.728		115.87	H
ATOM	9886	N	MET E	135	−6.274	33.436	−53.663		114.36	N
ATOM	9887	CA	MET E	135	−7.724	33.324	−53.753		116.92	C
ATOM	9888	C	MET E	135	−8.391	34.654	−53.402		116.18	C
ATOM	9889	O	MET E	135	−9.399	35.025	−54.011		114.50	O
ATOM	9890	CB	MET E	135	−8.230	32.199	−52.849		117.85	C
ATOM	9891	CG	MET E	135	−7.779	30.819	−53.309		116.72	C
ATOM	9892	SD	MET E	135	−8.442	30.370	−54.924		124.82	S
ATOM	9893	CE	MET E	135	−10.125	29.954	−54.479		172.84	C
ATOM	9894	H	MET E	135	−5.923	33.010	−53.003		117.23	H
ATOM	9895	HA	MET E	135	−7.959	33.093	−54.666		120.30	H
ATOM	9896	HB2	MET E	135	−7.892	32.341	−51.951		121.42	H
ATOM	9897	HB3	MET E	135	−9.200	32.211	−52.844		121.42	H
ATOM	9898	HG2	MET E	135	−6.811	30.806	−53.368		120.06	H
ATOM	9899	HG3	MET E	135	−8.080	30.158	−52.666		120.06	H
ATOM	9900	HE1	MET E	135	−10.606	29.688	−55.278		187.41	H
ATOM	9901	HE2	MET E	135	−10.111	29.222	−53.842		187.41	H
ATOM	9902	HE3	MET E	135	−10.548	30.731	−54.081		187.41	H
ATOM	9903	N	HIS E		136	−7.832	35.373	−52.432		111.58	N
ATOM	9904	CA	HIS E		136	−8.310	36.721	−52.129		114.06	C
ATOM	9905	C	HIS E		136	−8.086	37.640	−53.325		114.28	C
ATOM	9906	O	HIS E	136	−8.963	38.424	−53.693		117.87	O
ATOM	9907	CB	HIS E	136	−7.610	37.302	−50.899		112.00	C
ATOM	9908	CG	HIS E	136	−8.065	36.709	−49.603		116.23	C
ATOM	9909	ND1	HIS E	136	−8.066	37.421	−48.422		114.57	N
ATOM	9910	CD2	HIS E		136	−8.528	35.474	−49.298		114.11	C
ATOM	9911	CE1	HIS E	136	−8.511	36.650	−47.447		119.48	C
ATOM	9912	NE2	HIS E	136	−8.798	35.463	−47.952		116.55	N
ATOM	9913	H	HIS E		136	−7.180	35.107	−51.939		113.89	H
ATOM	9914	HA	HIS E	136	−9.262	36.688	−51.948		116.87	H
ATOM	9915	HB2	HIS E	136	−6.656	37.142	−50.979		114.40	H
ATOM	9916	HB3	HIS E	136	−7.780	38.256	−50.865		114.40	H
ATOM	9917	HD1	HIS E	136	−7.815	38.239	−48.334		117.48	H
ATOM	9918	HD2	HIS E		136	−8.642	34.765	−49.890		116.93	H
ATOM	9919	HE1	HIS E	136	−8.606	36.900	−46.556		123.37	H
ATOM	9920	HE2	HIS E		136	−9.106	34.793	−47.509		119.86	H
ATOM	9921		LEU E	137	−6.903	37.539	−53.922		113.80	N
ATOM	9922	CA	LEU E	137	−6.548	38.344	−55.086		114.11	C
ATOM	9923		LEU E	137	−7.567	38.163	−56.209		114.94	C
ATOM	9924	O	LEU E	137	−8.077	39.134	−56.758		116.40	O
ATOM	9925	CB	LEU E	137	−5.142	37.980	−55.573		113.09	C
ATOM	9926	CG	LEU E		137	−4.711	38.506	−56.945		115.68	C
ATOM	9927	CD1	LEU E	137	−4.834	40.023	−57.025		119.57	C
ATOM	9928	CD2	LEU E		137	−3.285	38.070	−57.252		116.15	C
ATOM	9929	H	LEU E	137	−6.280	37.003	−53.668		116.56	H
ATOM	9930	HA	LEU E	137	−6.545	39.281	−54.833		116.93	H
ATOM	9931	HB2	LEU E	137	−4.504	38.317	−54.925		115.71	H
ATOM	9932	HB3	LEU E	137	−5.079	37.012	−55.607		115.71	H
ATOM	9933	HG	LEU E	137	−5.290	38.125	−57.623		118.82	H
ATOM	9934	HD11	LEU E	137	−4.553	40.316	−57.906		123.48	H
ATOM	9935	HD12	LEU E	137	−5.759	40.272	−56.873		123.48	H
ATOM	9936	HD13	LEU E	137	−4.267	40.422	−56.346		123.48	H
ATOM	9937	HD21	LEU E	137	−3.031	38.412	−58.123		119.37	H
ATOM	9938	HD22	LEU E	137	−2.693	38.425	−56.570		119.37	H
ATOM	9939	HD23	LEU E	137	−3.245	37.100	−57.252		119.37	H
ATOM	9940	N	ARG E	138	−7.872	36.915	−56.536		115.03	N
ATOM	9941	CA	ARG E	138	−8.821	36.624	−57.599		117.21	C
ATOM	9942	C	ARG E	138	−10.223	37.129	−57.242		118.67	C
ATOM	9943	O	ARG E	138	−10.941	37.654	−58.093		117.07	O
ATOM	9944	CB	ARG E	138	−8.835	35.121	−57.883		117.26	C
ATOM	9945	CG	ARG E	138	−7.536	34.621	−58.502		118.09	C
ATOM	9946	CD	ARG E	138	−7.529	33.110	−58.664		122.76	C
ATOM	9947	NE	ARG E	138	−8.525	32.659	−59.628		125.06	N
ATOM	9948	CZ	ARG E	138	−8.955	31.407	−59.728		130.07	C
ATOM	9949	NH1	ARG E	138	−8.479	30.470	−58.918		128.66	N1+
ATOM	9950	NH2	ARG E	138	−9.870	31.092	−60.635		131.23	N
ATOM	9951	H	ARG E	138	−7.542	36.217	−56.156		118.04	H
ATOM	9952	HA	ARG E	138	−8.537	37.078	−58.408		120.66	H
ATOM	9953	HB2	ARG E	138	−8.973	34.644	−57.050		120.72	H
ATOM	9954	HB3	ARG E	138	−9.556	34.924	−58.501		120.72	H
ATOM	9955	HG2	ARG E	138	−7.426	35.020	−59.380		121.70	H
ATOM	9956	HG3	ARG E	138	−6.794	34.867	−57.928		121.70	H
ATOM	9957	HD2	ARG E	138	−6.655	32.828	−58.978		127.31	H
ATOM	9958	HD3	ARG E	138	−7.727	32.698	−57.809		127.31	H
ATOM	9959	HE	ARG E	138	−8.856	33.242	−60.167		130.07	H
ATOM	9960	HH11	ARG E	138	−7.888	30.673	−58.328		134.40	H
ATOM	9961	HH12	ARG E	138	−8.761	29.661	−58.985		134.40	H
ATOM	9962	HH21	ARG E	138	−10.180	31.697	−61.161		137.48	H
ATOM	9963	HH22	ARG E	138	−10.149	30.281	−60.700		137.48	H
ATOM	9964	N	SER E	139	−10.603	36.994	−55.978		116.32	N
ATOM	9965	CA	SER E	139	−11.907	37.474	−55.534		116.34	C
ATOM	9966	C	SER E	139	−11.968	39.002	−55.579		117.91	C
ATOM	9967	O	SER E	139	−13.011	39.582	−55.889		116.73	O
ATOM	9968	CB	SER E	139	−12.210	36.973	−54.121		115.40	C
ATOM	9969	OG	SER E	139	−12.117	35.559	−54.052		115.94	O
ATOM	9970	H	SER E	139	−10.129	36.630	−55.359		119.59	H
ATOM	9971	HA	SER E	139	−12.590	37.128	−56.129		119.61	H
ATOM	9972	HB2	SER E	139	−11.569	37.361	−53.504		118.47	H
ATOM	9973	HB3	SER E	139	−13.109	37.242	−53.877		118.47	H
ATOM	9974	HG	SER E	139	−12.668	35.209	−54.582		119.13	H
ATOM	9975	N	LEU E	140	−10.851	39.657	−55.274		116.92	N
ATOM	9976	CA	LEU E	140	−10.813	41.119	−55.262		116.54	C
ATOM	9977	C	LEU E	140	−10.772	41.679	−56.680		116.09	C
ATOM	9978	O	LEU E	140	−11.345	42.734	−56.953		120.02	O
ATOM	9979	CB	LEU E	140	−9.612	41.620	−54.459		114.74	C
ATOM	9980	CG	LEU E	140	−9.696	41.416	−52.944		113.44	C
ATOM	9981	CD1	LEU E	140	−8.341	41.666	−52.303		116.07	C
ATOM	9982	CD2	LEU E	140	−10.762	42.310	−52.316		117.46	C
ATOM	9983	H	LEU E	140	−10.105	39.281	−55.070		120.30	H
ATOM	9984	HA	LEU E	140	−11.617	41.450	−54.834		119.85	H
ATOM	9985	HB2	LEU E	140	−8.820	41.157	−54.771		117.68	H
ATOM	9986	HB3	LEU E	140	−9.514	42.572	−54.618		117.68	H
ATOM	9987	HG	LEU E	140	−9.941	40.494	−52.766		116.13	H
ATOM	9988	HD11	LEU E	140	−8.415	41.532	−51.346		119.28	H
ATOM	9989	HD12	LEU E	140	−7.696	41.045	−52.676		119.28	H
ATOM	9990	HD13	LEU E	140	−8.068	42.578	−52.490		119.28	H
ATOM	9991	HD21	LEU E	140	−10.784	42.151	−51.359		120.95	H
ATOM	9992	HD22	LEU E	140	−10.540	43.238	−52.493		120.95	H
ATOM	9993	HD23	LEU E	140	−11.624	42.096	−52.707		120.95	H
ATOM	9994	N	VAL E	141	−10.099	40.975	−57.583		119.49	N
ATOM	9995	CA	VAL E	141	−10.106	41.360	−58.987		119.08	C
ATOM	9996	C	VAL E	141	−11.545	41.319	−59.499		121.59	C
ATOM	9997	O	VAL E	141	−11.956	42.169	−60.284		125.99	O
ATOM	9998	CB	VAL E	141	−9.200	40.441	−59.836		119.66	C
ATOM	9999	CG1	VAL E	141	−9.450	40.649	−61.326		122.61	C
ATOM	10000	CG2	VAL E	141	−7.733	40.702	−59.517		118.87	C
ATOM	10001	H	VAL E	141	−9.633	40.274	−57.409		123.39	H
ATOM	10002	HA	VAL E	141	−9.779	42.270	−59.071		122.90	H
ATOM	10003	HB	VAL E	141	−9.396	39.515	−59.623		123.59	H
ATOM	10004	HG11	VAL E	141	−8.868	40.059	−61.829		127.13	H
ATOM	10005	HG12	VAL E	141	−10.378	40.445	−61.522		127.13	H
ATOM	10006	HG13	VAL E	141	−9.260	41.573	−61.551		127.13	H
ATOM	10007	HG21	VAL E	141	−7.183	40.116	−60.059		122.64	H
ATOM	10008	HG22	VAL E	141	−7.528	41.629	−59.717		122.64	H
ATOM	10009	HG23	VAL E	141	−7.579	40.525	−58.576		122.64	H
ATOM	10010	N	ARG E	142	−12.307	40.335	−59.033		119.07	N
ATOM	10011	CA	ARG E	142	−13.704	40.192	−59.429		124.24	C
ATOM	10012	C	ARG E	142	−14.533	41.405	−59.009		126.35	C
ATOM	10013	O	ARG E	142	−15.269	41.966	−59.821		128.20	O
ATOM	10014	CB	ARG E	142	−14.294	38.913	−58.832		125.76	C
ATOM	10015	CG	ARG E	142	−15.783	38.721	−59.070		136.68	C
ATOM	10016	CD	ARG E	142	−16.117	38.625	−60.548		144.40	C
ATOM	10017	NE	ARG E	142	−17.545	38.399	−60.761		154.59	N
ATOM	10018	CZ	ARG E	142	−18.135	37.208	−60.717		159.95	C
ATOM	10019	NH1	ARG E	142	−17.425	36.115	−60.469		156.87	N1+
ATOM	10020	NH2	ARG E	142	−19.440	37.109	−60.921		168.51	N
ATOM	10021	H	ARG E	142	−12.037	39.733	−58.483		122.89	H
ATOM	10022	HA	ARG E	142	−13.751	40.119	−60.395		129.09	H
ATOM	10023	HB2	ARG E	142	−13.835	38.151	−59.219		130.91	H
ATOM	10024	HB3	ARG E	142	−14.150	38.925	−57.872		130.91	H
ATOM	10025	HG2	ARG E	142	−16.071	37.900	−58.641		144.02	H
ATOM	10026	HG3	ARG E	142	−16.265	39.478	−58.700		144.02	H
ATOM	10027	HD2	ARG E	142	−15.872	39.455	−60.986		153.28	H
ATOM	10028	HD3	ARG E	142	−15.631	37.882	−60.939		153.28	H
ATOM	10029	HE	ARG E	142	−18.038	39.084	−60.927		165.51	H
ATOM	10030	HH11	ARG E	142	−16.578	36.173	−60.334		168.25	H
ATOM	10031	HH12	ARG E	142	−17.813	35.347	−60.442		168.25	H
ATOM	10032	HH21	ARG E	142	−19.905	37.814	−61.084		182.22	H
ATOM	10033	HH22	ARG E	142	−19.822	36.339	−60.894		182.22	H
ATOM	10034	N	LYS E	143	−14.416	41.805	−57.745		123.88	N
ATOM	10035	CA	LYS E	143	−15.118	42.986	−57.251		128.82	C
ATOM	10036	C	LYS E	143	−14.736	44.212	−58.065		128.57	C
ATOM	10037	O	LYS E	143	−15.592	44.986	−58.488		131.07	O
ATOM	10038	CB	LYS E	143	−14.800	43.246	−55.778		123.54	C
ATOM	10039	CG	LYS E	143	−15.219	42.147	−54.829		128.69	C
ATOM	10040	CD	LYS E	143	−15.096	42.597	−53.378		128.36	C
ATOM	10041	CE	LYS E	143	−16.233	43.528	−52.982		135.13	C
ATOM	10042	NZ	LYS E	143	−16.120	43.988	−51.571		139.13	N1+
ATOM	10043	H	LYS E	143	−13.935	41.408	−57.152		128.66	H
ATOM	10044	HA	LYS E	143	−16.074	42.849	−57.337		134.59	H
ATOM	10045	HB2	LYS E	143	−13.842	43.363	−55.685		128.25	H
ATOM	10046	HB3	LYS E	143	−15.255	44.057	−55.503		128.25	H
ATOM	10047	HG2	LYS E	143	−16.144	41.911	−54.998		134.42	H
ATOM	10048	HG3	LYS E	143	−14.645	41.375	−54.959		134.42	H
ATOM	10049	HD2	LYS E	143	−15.124	41.819	−52.799		134.03	H
ATOM	10050	HD3	LYS E	143	−14.259	43.072	−53.261		134.03	H
ATOM	10051	HE2	LYS E	143	−16.218	44.309	−53.557		142.15	H
ATOM	10052	HE3	LYS E	143	−17.076	43.059	−53.080		142.15	H
ATOM	10053	HZ1	LYS E	143	−16.137	43.289	−51.021		146.95	H
ATOM	10054	HZ2	LYS E	143	−15.355	44.429	−51.455		146.95	H
ATOM	10055	HZ3	LYS E	143	−16.798	44.529	−51.372		146.95	H
ATOM	10056	N	MET E	144	−13.436	44.376	−58.272		125.28	N
ATOM	10057	CA	MET E	144	−12.900	45.547	−58.948		127.97	C
ATOM	10058	C	MET E	144	−13.406	45.645	−60.384		135.15	C
ATOM	10059	O	MET E	144	−13.712	46.735	−60.871		134.51	O
ATOM	10060	CB	MET E	144	−11.370	45.506	−58.919		125.24	C
ATOM	10061	CG	MET E	144	−10.688	46.653	−59.650		129.40	C
ATOM	10062	SD	MET E	144	−10.298	46.242	−61.360		142.62	S
ATOM	10063	CE	MET E	144	−9.018	45.007	−61.143		135.57	C
ATOM	10064	H	MET E	144	−12.835	43.813	−58.026		130.34	H
ATOM	10065	HA	MET E	144	−13.182	46.340	−58.465		133.56	H
ATOM	10066	HB2	MET E	144	−11.078	45.533	−57.994		130.28	H
ATOM	10067	HB3	MET E	144	−11.076	44.679	−59.330		130.28	H
ATOM	10068	HG2	MET E	144	−11.278	47.423	−59.653		135.29	H
ATOM	10069	HG3	MET E	144	−9.859	46.870	−59.196		135.29	H
ATOM	10070	HE1	MET E	144	−8.721	44.703	−62.015		142.68	H
ATOM	10071	HE2	MET E	144	−8.276	45.403	−60.660		142.68	H
ATOM	10072	HE3	MET E	144	−9.381	44.262	−60.639		142.68	H
ATOM	10073	N	GLU E	145	−13.501	44.505	−61.059		131.93	N
ATOM	10074	CA	GLU E	145	−13.949	44.488	−62.446		131.71	C
ATOM	10075	C	GLU E	145	−15.462	44.676	−62.551		130.25	C
ATOM	10076	O	GLU E	145	−15.959	45.154	−63.568		133.30	O
ATOM	10077	CB	GLU E	145	−13.522	43.186	−63.125		133.36	C
ATOM	10078	CG	GLU E	145	−12.021	43.118	−63.401		135.77	C
ATOM	10079	CD	GLU E	145	−11.606	41.844	−64.115		137.01	C
ATOM	10080	OE1	GLU E	145	−12.430	40.908	−64.196		136.72	O
ATOM	10081	OE2	GLU E	145	−10.454	41.782	−64.598		137.94	O1−
ATOM	10082	H	GLU E	145	−13.313	43.729	−60.738		138.32	H
ATOM	10083	HA	GLU E	145	−13.526	45.222	−62.919		138.05	H
ATOM	10084	HB2	GLU E	145	−13.754	42.440	−62.550		140.04	H
ATOM	10085	HB3	GLU E	145	−13.986	43.107	−63.973		140.04	H
ATOM	10086	HG2	GLU E	145	−11.769	43.869	−63.960		142.93	H
ATOM	10087	HG3	GLU E	145	−11.544	43.157	−62.558		142.93	H
ATOM	10088	N	ASP E	146	−16.188	44.314	−61.498		133.13	N
ATOM	10089	CA	ASP E	146	−17.638	44.488	−61.473		133.34	C
ATOM	10090	C	ASP E	146	−18.047	45.808	−60.815		139.24	C
ATOM	10091	O	ASP E	146	−19.225	46.021	−60.525		145.17	O
ATOM	10092	CB	ASP E	146	−18.306	43.323	−60.738		133.65	C
ATOM	10093	CG	ASP E	146	−18.110	41.998	−61.444		138.71	C
ATOM	10094	OD1	ASP E	146	−17.633	42.000	−62.600		144.37	O
ATOM	10095	OD2	ASP E	146	−18.444	40.953	−60.846		137.49	O1−
ATOM	10096	H	ASP E	146	−15.864	43.964	−60.782		139.75	H
ATOM	10097	HA	ASP E	146	−17.969	44.495	−62.385		140.00	H
ATOM	10098	HB2	ASP E	146	−17.924	43.249	−59.850		140.39	H
ATOM	10099	HB3	ASP E	146	−19.259	43.492	−60.677		140.39	H
ATOM	10100	N	SER E	147	−17.081	46.693	−60.585		136.27	N
ATOM	10101	CA	SER E	147	−17.357	47.964	−59.919		139.56	C
ATOM	10102	C	SER E	147	−18.193	48.896	−60.799		140.84	C
ATOM	10103	O	SER E	147	−17.812	49.204	−61.926		141.91	O
ATOM	10104	CB	SER E	147	−16.049	48.657	−59.528		140.67	C
ATOM	10105	OG	SER E	147	−16.299	49.901	−58.895		139.95	O
ATOM	10106	H	SER E	147	−16.257	46.582	−60.805		143.52	H
ATOM	10107	HA	SER E	147	−17.859	47.792	−59.107		147.47	H
ATOM	10108	HB2	SER E	147	−15.561	48.084	−58.916		148.80	H
ATOM	10109	HB3	SER E	147	−15.523	48.811	−60.329		148.80	H
ATOM	10110	HG	SER E	147	−15.573	50.269	−58.687		147.94	H
ATOM	10111	N	LYS E	148	−19.326	49.349	−60.270		144.08	N
ATOM	10112	CA	LYS E	148	−20.219	50.241	−61.006		149.92	C
ATOM	10113	C	LYS E	148	−19.658	51.658	−61.121		148.76	C
ATOM	10114	O	LYS E	148	−20.209	52.494	−61.838		151.47	O
ATOM	10115	CB	LYS E	148	−21.595	50.281	−60.339		147.47	C
ATOM	10116	CG	LYS E	148	−22.494	49.113	−60.710		150.15	C
ATOM	10117	CD	LYS E	148	−23.784	49.125	−59.908		147.36	C
ATOM	10118	CE	LYS E	148	−24.808	48.165	−60.488		150.24	C
ATOM	10119	NZ	LYS E	148	−24.266	46.787	−60.642		151.53	N1+
ATOM	10120	H	LYS E	148	−19.603	49.153	−59.479		152.90	H
ATOM	10121	HA	LYS E	148	−20.335	49.894	−61.905		159.91	H
ATOM	10122	HB2	LYS E	148	−21.476	50.269	−59.376		156.96	H
ATOM	10123	HB3	LYS E	148	−22.047	51.098	−60.604		156.96	H
ATOM	10124	HG2	LYS E	148	−22.721	49.170	−61.651		160.18	H
ATOM	10125	HG3	LYS E	148	−22.029	48.282	−60.526		160.18	H
ATOM	10126	HD2	LYS E	148	−23.596	48.855	−58.995		156.83	H
ATOM	10127	HD3	LYS E	148	−24.162	50.018	−59.922		156.83	H
ATOM	10128	HE2	LYS E	148	−25.575	48.123	−59.896		160.29	H
ATOM	10129	HE3	LYS E	148	−25.079	48.481	−61.364		160.29	H
ATOM	10130	HZ1	LYS E	148	−24.890	46.252	−60.983		161.84	H
ATOM	10131	HZ2	LYS E	148	−23.562	46.796	−61.187		161.84	H
ATOM	10132	HZ3	LYS E	148	−24.014	46.470	−59.850		161.84	H
ATOM	10133	N	ARG E	149	−18.566	51.925	−60.411		153.83	N
ATOM	10134	CA	ARG E	149	−17.911	53.229	−60.464		158.71	C
ATOM	10135	C	ARG E	149	−17.092	53.366	−61.747		157.83	C
ATOM	10136	O	ARG E	149	−17.518	54.015	−62.704		157.91	O
ATOM	10137	CB	ARG E	149	−17.015	53.422	−59.237		155.33	C
ATOM	10138	CG	ARG E	149	−16.391	54.807	−59.099		152.08	C
ATOM	10139	CD	ARG E	149	−17.379	55.834	−58.558		150.40	C
ATOM	10140	NE	ARG E	149	−16.679	56.984	−57.985		149.43	N
ATOM	10141	CZ	ARG E	149	−16.619	57.279	−56.687		145.97	C
ATOM	10142	NH1	ARG E	149	−17.237	56.531	−55.780		136.16	N1+
ATOM	10143	NH2	ARG E	149	−15.943	58.348	−56.292		150.80	N
ATOM	10144	H	ARG E	149	−18.180	51.363	−59.887		164.60	H
ATOM	10145	HA	ARG E	149	−18.586	53.925	−60.460		170.45	H
ATOM	10146	HB2	ARG E	149	−17.545	53.260	−58.441		166.39	H
ATOM	10147	HB3	ARG E	149	−16.291	52.779	−59.281		166.39	H
ATOM	10148	HG2	ARG E	149	−15.641	54.757	−58.486		162.50	H
ATOM	10149	HG3	ARG E	149	−16.091	55.108	−59.971		162.50	H
ATOM	10150	HD2	ARG E	149	−17.944	56.150	−59.280		160.48	H
ATOM	10151	HD3	ARG E	149	−17.917	55.427	−57.861		160.48	H
ATOM	10152	HE	ARG E	149	−16.273	57.511	−58.530		159.32	H
ATOM	10153	HH11	ARG E	149	−17.678	55.834	−56.025		143.39	H
ATOM	10154	HH12	ARG E	149	−17.191	56.739	−54.947		143.39	H
ATOM	10155	HH21	ARG E	149	−15.543	58.842	−56.871		160.96	H
ATOM	10156	HH22	ARG E	149	−15.906	58.549	−55.457		160.96	H
TER	10157		ARG E	149					1
ATOM	10158	N	GLY F	0	−3.228	29.760	20.619		129.41	N
ATOM	10159	CA	GLY F	0	−3.768	30.515	19.453		126.44	C
ATOM	10160	C	GLY F	0	−4.157	29.577	18.329		126.73	C
ATOM	10161	O	GLY F	0	−4.379	28.388	18.561		125.80	O
ATOM	10162	H1	GLY F	0	−3.701	29.959	21.346		135.29	H
ATOM	10163	H2	GLY F	0	−3.283	28.886	20.459		135.29	H
ATOM	10164	H3	GLY F	0	−2.376	29.984	20.750		135.29	H
ATOM	10165	HA2	GLY F	0	−4.551	31.019	19.723		131.73	H
ATOM	10166	HA3	GLY F	0	−3.097	31.133	19.124		131.73	H
ATOM	10167	N	HIS F		1	−4.237	30.106	17.110		121.94	N
ATOM	10168	CA	HIS F		1	−4.640	29.302	15.960		120.81	C
ATOM	10169	C	HIS F	1	−3.752	29.565	14.754		120.41	C
ATOM	10170	O	HIS F		1	−3.175	30.643	14.618		118.02	O
ATOM	10171	CB	HIS F		1	−6.099	29.577	15.600		119.93	C
ATOM	10172	CG	HIS F		1	−7.065	29.227	16.687		124.76	C
ATOM	10173	ND1	HIS F	1	−7.406	27.926	16.989		125.09	N
ATOM	10174	CD2	HIS F		1	−7.762	30.008	17.546		126.11	C
ATOM	10175	CE1	HIS F		1	−8.273	27.921	17.986		127.35	C
ATOM	10176	NE2	HIS F	1	−8.505	29.171	18.343		127.19	N
ATOM	10177	H	HIS F		1	−4.063	30.927	16.923		126.33	H
ATOM	10178	HA	HIS F		1	−4.561	28.363	16.190		124.97	H
ATOM	10179	HB2	HIS F	1	−6.200	30.522	15.405		123.91	H
ATOM	10180	HB3	HIS F	1	−6.331	29.053	14.817		123.91	H
ATOM	10181	HD1	HIS F	1	−7.103	27.227	16.590		130.10	H
ATOM	10182	HD2	HIS F		1	−7.742	30.937	17.589		131.34	H
ATOM	10183	HE1	HIS F		1	−8.654	27.166	18.372		132.82	H
ATOM	10184	HE2	HIS F		1	−9.036	29.421	18.972		132.63	H
ATOM	10185	N	LYS F	2	−3.635	28.568	13.884		117.59	N
ATOM	10186	CA	LYS F	2	−2.874	28.734	12.658		118.28	C
ATOM	10187	C	LYS F	2	−3.516	27.985	11.498		119.46	C
ATOM	10188	O	LYS F	2	−4.114	26.920	11.668		115.97	O
ATOM	10189	CB	LYS F	2	−1.424	28.284	12.858		121.88	C
ATOM	10190	CG	LYS F	2	−1.243	26.852	13.311		129.22	C
ATOM	10191	CD	LYS F	2	0.205	26.606	13.713		130.79	C
ATOM	10192	CE	LYS F	2	0.429	25.175	14.167		140.64	C
ATOM	10193	NZ	LYS F	2	1.839	24.947	14.592		146.99	N1+
ATOM	10194	H	LYS F	2	−3.985	27.788	13.982		121.11	H
ATOM	10195	HA	LYS F	2	−2.861	29.676	12.428		121.93	H
ATOM	10196	HB2	LYS F	2	−0.953	28.385	12.017		126.26	H
ATOM	10197	HB3	LYS F	2	−1.015	28.855	13.528		126.26	H
ATOM	10198	HG2	LYS F	2	−1.810	26.681	14.079		135.07	H
ATOM	10199	HG3	LYS F	2	−1.467	26.252	12.583		135.07	H
ATOM	10200	HD2	LYS F	2	0.781	26.775	12.951		136.94	H
ATOM	10201	HD3	LYS F	2	0.438	27.196	14.446		136.94	H
ATOM	10202	HE2	LYS F	2	−0.150	24.985	14.921		148.77	H
ATOM	10203	HE3	LYS F	2	0.233	24.573	13.433		148.77	H
ATOM	10204	HZ1	LYS F	2	2.043	25.487	15.270		156.39	H
ATOM	10205	HZ2	LYS F	2	1.944	24.103	14.854		156.39	H
ATOM	10206	HZ3	LYS F	2	2.391	25.111	13.914		156.39	H
ATOM	10207	N	LEU F	3	−3.404	28.589	10.321		118.68	N
ATOM	10208	CA	LEU F	3	−3.925	28.030	9.086		117.42	C
ATOM	10209	C	LEU F	3	−2.752	27.857	8.134		116.58	C
ATOM	10210	O	LEU F	3	−2.066	28.828	7.807		115.05	O
ATOM	10211	CB	LEU F	3	−4.995	28.945	8.485		115.28	C
ATOM	10212	CG	LEU F		3	−5.747	28.440	7.256		118.11	C
ATOM	10213	CD1	LEU F	3	−6.670	27.286	7.622		117.93	C
ATOM	10214	CD2	LEU F		3	−6.527	29.581	6.615		115.66	C
ATOM	10215	H	LEU F	3	−3.016	29.349	10.212		122.41	H
ATOM	10216	HA	LEU F		3	−4.319	27.160	9.258		120.90	H
ATOM	10217	HB2	LEU F	3	−5.657	29.121	9.171		118.34	H
ATOM	10218	HB3	LEU F	3	−4.568	29.779	8.234		118.34	H
ATOM	10219	HG	LEU F	3	−5.105	28.115	6.606		121.73	H
ATOM	10220	HD11	LEU F	3	−7.134	26.987	6.824		121.52	H
ATOM	10221	HD12	LEU F	3	−6.139	26.561	7.987		121.52	H
ATOM	10222	HD13	LEU F	3	−7.312	27.592	8.282		121.52	H
ATOM	10223	HD21	LEU F	3	−6.998	29.243	5.837		118.80	H
ATOM	10224	HD22	LEU F	3	−7.162	29.931	7.260		118.80	H
ATOM	10225	HD23	LEU F	3	−5.906	30.278	6.349		118.80	H
ATOM	10226	N	ALA F	4	−2.520	26.620	7.706		117.17	N
ATOM	10227	CA	ALA F	4	−1.347	26.278	6.911		113.80	C
ATOM	10228	C	ALA F	4	−1.737	25.668	5.570		118.72	C
ATOM	10229	O	ALA F	4	−2.616	24.807	5.492		115.41	O
ATOM	10230	CB	ALA F	4	−0.455	25.321	7.681		116.99	C
ATOM	10231	H	ALA F	4	−3.037	25.951	7.865		120.60	H
ATOM	10232	HA	ALA F	4	−0.839	27.085	6.736		116.56	H
ATOM	10233	HB1	ALA F	4	0.319	25.105	7.138		120.38	H
ATOM	10234	HB2	ALA F	4	−0.172	25.747	8.506		120.38	H
ATOM	10235	HB3	ALA F	4	−0.955	24.514	7.880		120.38	H
ATOM	10236	N	PHE F	5	−1.065	26.132	4.522		114.07	N
ATOM	10237	CA	PHE F	5	−1.247	25.619	3.171		115.88	C
ATOM	10238	C	PHE F	5	0.038	24.967	2.696		117.08	C
ATOM	10239	O	PHE F	5	1.085	25.610	2.658		119.17	O
ATOM	10240	CB	PHE F	5	−1.642	26.742	2.213		111.34	C
ATOM	10241	CG	PHE F	5	−2.919	27.422	2.580		110.85	C
ATOM	10242	CD1	PHE F	5	−2.940	28.405	3.554		113.28	C
ATOM	10243	CD2	PHE F	5	−4.100	27.084	1.953		112.14	C
ATOM	10244	CE1	PHE F	5	−4.120	29.036	3.893		113.84	C
ATOM	10245	CE2	PHE F	5	5.280	27.712	2.288		111.37	C
ATOM	10246	CZ	PHE F	5	−5.291	28.686	3.258		114.78	C
ATOM	10247	H	PHE F	5	−0.481	26.761	4.571		116.89	H
ATOM	10248	HA	PHE F		5	−1.951	24.952	3.169		119.06	H
ATOM	10249	HB2	PHE F	5	−0.940	27.411	2.209		113.61	H
ATOM	10250	HB3	PHE F	5	−1.749	26.371	1.323		113.61	H
ATOM	10251	HD1	PHE F	5	−2.151	28.643	3.984		115.93	H
ATOM	10252	HD2	PHE F	5	−4.100	26.425	1.296		114.56	H
ATOM	10253	HE1	PHE F	5	−4.124	29.695	4.549		116.61	H
ATOM	10254	HE2	PHE F	5	−6.070	27.475	1.859		113.65	H
ATOM	10255	HZ	PHE F	5	−6.087	29.109	3.484		117.73	H
ATOM	10256	N	ASN F	6	−0.047	23.691	2.336		116.88	N
ATOM	10257	CA	ASN F	6	1.106	22.963	1.838		114.07	C
ATOM	10258	C	ASN F	6	0.919	22.591	0.376		116.67	C
ATOM	10259	O	ASN F	6	0.153	21.682	0.056		116.36	O
ATOM	10260	CB	ASN F	6	1.348	21.713	2.679		120.64	C
ATOM	10261	CG	ASN F	6	2.626	21.000	2.300		126.49	C
ATOM	10262	OD1	ASN F	6	2.607	20.029	1.548		133.61	O
ATOM	10263	ND2	ASN F	6	3.748	21.486	2.814		126.66	N
ATOM	10264	H	ASN F	6	−0.768	23.223	2.373		120.26	H
ATOM	10265	HA	ASN F	6	1.892	23.528	1.906		116.89	H
ATOM	10266	HB2	ASN F	6	1.411	21.966	3.613		124.77	H
ATOM	10267	HB3	ASN F	6	0.611	21.096	2.550		124.77	H
ATOM	10268	HD21	ASN F	6	4.502	21.116	2.629		132.00	H
ATOM	10269	HD22	ASN F	6	3.722	22.171	3.333		132.00	H
ATOM	10270	N	PHE F	7	1.618	23.318	−0.497		114.97	N
ATOM	10271	CA	PHE F	7	1.580	23.101	−1.939		112.47	C
ATOM	10272	C	PHE F	7	2.716	22.190	−2.376		115.61	C
ATOM	10273	O	PHE F	7	3.871	22.427	−2.029		116.76	O
ATOM	10274	CB	PHE F	7	1.695	24.426	−2.696		112.90	C
ATOM	10275	CG	PHE F	7	0.586	25.391	−2.415		112.41	C
ATOM	10276	CD1	PHE F	7	0.627	26.208	−1.299		115.02	C
ATOM	10277	CD2	PHE F	7	−0.491	25.494	−3.277		113.17	C
ATOM	10278	CE1	PHE F		7	−0.392	27.108	−1.041		114.33	C
ATOM	10279	CE2	PHE F		7	−1.516	26.392	−3.023		115.79	C
ATOM	10280	CZ	PHE F	7	−1.463	27.200	−1.902		114.48	C
ATOM	10281	H	PHE F	7	2.138	23.963	−0.267		117.96	H
ATOM	10282	HA	PHE F	7	0.739	22.681	−2.180		114.96	H
ATOM	10283	HB2	PHE F	7	2.529	24.855	−2.448		115.48	H
ATOM	10284	HB3	PHE F	7	1.692	24.242	−3.649		115.48	H
ATOM	10285	HD1	PHE F	7	1.348	26.150	−0.714		118.02	H
ATOM	10286	HD2	PHE F	7	−0.530	24.953	−4.032		115.81	H
ATOM	10287	HE1	PHE F	7	−0.355	27.649	−0.285		117.19	H
ATOM	10288	HE2	PHE F		7	−2.238	26.452	−3.607		118.95	H
ATOM	10289	HZ	PHE F	7	−2.150	27.803	−1.729		117.38	H
ATOM	10290	N	ASN F	8	2.390	21.165	−3.153		117.16	N
ATOM	10291	CA	ASN F	8	3.399	20.249	−3.662		118.00	C
ATOM	10292	C	ASN F	8	3.214	19.985	−5.147		119.06	C
ATOM	10293	O	ASN F	8	2.111	19.667	−5.601		119.50	O
ATOM	10294	CB	ASN F	8	3.363	18.931	−2.891		121.59	C
ATOM	10295	CG	ASN F	8	4.399	17.940	−3.386		125.54	C
ATOM	10296	OD1	ASN F	8	4.066	16.957	−4.047		128.38	O
ATOM	10297	ND2	ASN F	8	5.664	18.203	−3.080		127.01	N
ATOM	10298	H	ASN F	8	1.588	20.978	−3.400		120.60	H
ATOM	10299	HA	ASN F	8	4.275	20.645	−3.536		121.60	H
ATOM	10300	HB2	ASN F	8	3.540	19.108	−1.953		125.91	H
ATOM	10301	HB3	ASN F	8	2.487	18.527	−2.993		125.91	H
ATOM	10302	HD21	ASN F	8	6.288	17.671	−3.338		132.41	H
ATOM	10303	HD22	ASN F	8	5.859	18.906	−2.624		132.41	H
ATOM	10304	N	LEU F	9	4.302	20.141	−5.894		117.68	N
ATOM	10305	CA	LEU F	9	4.342	19.779	−7.306		118.16	C
ATOM	10306	C	LEU F	9	5.423	18.732	−7.510		119.22	C
ATOM	10307	O	LEU F	9	6.607	19.007	−7.327		116.70	O
ATOM	10308	CB	LEU F	9	4.610	21.001	−8.190		112.54	C
ATOM	10309	CG	LEU F	9	4.756	20.712	−9.690		115.42	C
ATOM	10310	CD1	LEU F	9	3.456	20.192	−10.273		121.54	C
ATOM	10311	CD2	LEU F	9	5.212	21.955	−10.437		117.32	C
ATOM	10312	H	LEU F	9	5.044	20.461	−5.600		121.21	H
ATOM	10313	HA	LEU F	9	3.490	19.395	−7.564		121.79	H
ATOM	10314	HB2	LEU F	9	3.874	21.624	−8.084		115.05	H
ATOM	10315	HB3	LEU F	9	5.434	21.419	−7.893		115.05	H
ATOM	10316	HG	LEU F	9	5.431	20.027	−9.813		118.50	H
ATOM	10317	HD11	LEU F	9	3.581	20.020	−11.219		125.85	H
ATOM	10318	HD12	LEU F	9	3.211	19.372	−9.816		125.85	H
ATOM	10319	HD13	LEU F	9	2.764	20.860	−10.146		125.85	H
ATOM	10320	HD21	LEU F	9	5.295	21.744	−11.380		120.79	H
ATOM	10321	HD22	LEU F	9	4.554	22.657	−10.312		120.79	H
ATOM	10322	HD23	LEU F	9	6.070	22.238	−10.084		120.79	H
ATOM	10323	N	GLU F	10	4.995	17.529	−7.874		121.49	N
ATOM	10324	CA	GLU F	10	5.898	16.421	−8.146		123.67	C
ATOM	10325	C	GLU F	10	6.031	16.251	−9.654		124.38	C
ATOM	10326	O	GLU F	10	5.045	15.994	−10.343		121.67	O
ATOM	10327	CB	GLU F	10	5.380	15.135	−7.494		128.50	C
ATOM	10328	CG	GLU F	10	6.252	13.911	−7.718		139.90	C
ATOM	10329	CD	GLU F	10	5.703	12.675	−7.023		146.88	C
ATOM	10330	OE1	GLU F	10	5.964	11.553	−7.505		153.49	O
ATOM	10331	OE2	GLU F	10	5.010	12.825	−5.994		153.38	O1−
ATOM	10332	H	GLU F	10	4.165	17.326	−7.973		125.79	H
ATOM	10333	HA	GLU F	10	6.775	16.620	−7.780		128.41	H
ATOM	10334	HB2	GLU F	10	5.316	15.279	−6.537		134.20	H
ATOM	10335	HB3	GLU F	10	4.501	14.939	−7.854		134.20	H
ATOM	10336	HG2	GLU F	10	6.301	13.726	−8.668		147.88	H
ATOM	10337	HG3	GLU F	10	7.139	14.085	−7.366		147.88	H
ATOM	10338	N	ILE F	11	7.251	16.419	−10.156		123.21	N
ATOM	10339	CA	ILE F	11	7.533	16.310	−11.584		125.02	C
ATOM	10340	C	ILE F	11	8.327	15.040	−11.859		129.40	C
ATOM	10341	O	ILE F	11	9.479	14.924	−11.444		128.51	O
ATOM	10342	CB	ILE F	11	8.328	17.527	−12.103		122.20	C
ATOM	10343	CG1	ILE F	11	7.615	18.831	−11.736		124.16	C
ATOM	10344	CG2	ILE F	11	8.526	17.429	−13.613		124.02	C
ATOM	10345	CD1	ILE F	11	8.442	20.071	−11.975		125.01	C
ATOM	10346	H	ILE F	11	7.945	16.600	−9.681		127.85	H
ATOM	10347	HA	ILE F	11	6.697	16.260	−12.073		130.03	H
ATOM	10348	HB	ILE F	11	9.200	17.526	−11.679		126.63	H
ATOM	10349	HG12	ILE F	11	6.808	18.906	−12.270		128.88	H
ATOM	10350	HG13	ILE F	11	7.384	18.806	−10.794		128.99	H
ATOM	10351	HG21	ILE F	11	9.027	18.203	−13.916		128.83	H
ATOM	10352	HG22	ILE F	11	9.016	16.617	−13.815		128.83	H
ATOM	10353	HG23	ILE F	11	7.657	17.408	−14.044		128.83	H
ATOM	10354	HD11	ILE F	11	7.923	20.850	−11.720		130.01	H
ATOM	10355	HD12	ILE F	11	9.248	20.020	−11.438		130.01	H
ATOM	10356	HD13	ILE F	11	8.672	20.120	−12.916		130.01	H
ATOM	10357	N	ASN F	12	7.703	14.090	−12.549		132.32	N
ATOM	10358	CA	ASN F	12	8.372	12.856	−12.939		139.08	C
ATOM	10359	C	ASN F	12	8.394	12.742	−14.461		141.01	C
ATOM	10360	O	ASN F	12	7.444	12.261	−15.081		132.24	O
ATOM	10361	CB	ASN F	12	7.683	11.646	−12.306		142.36	C
ATOM	10362	CG	ASN F	12	8.618	10.462	−12.149		149.52	C
ATOM	10363	OD1	ASN F	12	9.445	10.190	−13.019		151.85	O
ATOM	10364	ND2	ASN F	12	8.501	9.760	−11.027		149.58	N
ATOM	10365	H	ASN F	12	6.884	14.138	−12.805		138.78	H
ATOM	10366	HA	ASN F	12	9.289	12.879	−12.625		146.89	H
ATOM	10367	HB2	ASN F	12	7.358	11.891	−11.426		150.83	H
ATOM	10368	HB3	ASN F	12	6.943	11.372	−12.870		150.83	H
ATOM	10369	HD21	ASN F	12	9.008	9.079	−10.891		159.50	H
ATOM	10370	HD22	ASN F	12	7.918	9.986	−10.437		159.50	H
ATOM	10371	N	GLY F	13	9.490	13.206	−15.057		143.87	N
ATOM	10372	CA	GLY F	13	9.594	13.288	−16.500		137.61	C
ATOM	10373	C	GLY F	13	8.548	14.247	−17.031		134.27	C
ATOM	10374	O	GLY F	13	8.500	15.409	−16.628		138.41	O
ATOM	10375	H	GLY F	13	10.190	13.479	−14.639		152.65	H
ATOM	10376	HA2	GLY F	13	10.474	13.609	−16.752		145.13	H
ATOM	10377	HA3	GLY F	13	9.451	12.414	−16.895		145.13	H
ATOM	10378	N	SER F	14	7.700	13.754	−17.927		132.43	N
ATOM	10379	CA	SER F	14	6.603	14.550	−18.467		138.16	C
ATOM	10380	C	SER F	14	5.368	14.442	−17.574		138.46	C
ATOM	10381	O	SER F	14	4.368	15.130	−17.790		134.82	O
ATOM	10382	CB	SER F	14	6.270	14.101	−19.894		140.70	C
ATOM	10383	OG	SER F	14	5.954	12.720	−19.938		140.46	O
ATOM	10384	H	SER F	14	7.739	12.955	−18.242		138.92	H
ATOM	10385	HA	SER F	14	6.872	15.481	−18.499		145.79	H
ATOM	10386	HB2	SER F	14	5.508	14.609	−20.213		148.84	H
ATOM	10387	HB3	SER F	14	7.038	14.266	−20.462		148.84	H
ATOM	10388	HG	SER F	14	5.288	12.562	−19.450		148.55	H
ATOM	10389	N	ASP F	15	5.451	13.578	−16.567		136.67	N
ATOM	10390	CA	ASP F	15	4.350	13.349	−15.640		137.21	C
ATOM	10391	C	ASP F	15	4.410	14.336	−14.473		136.51	C
ATOM	10392	O	ASP F	15	5.475	14.545	−13.888		127.52	O
ATOM	10393	CB	ASP F	15	4.402	11.911	−15.119		143.65	C
ATOM	10394	CG	ASP F	15	3.030	11.302	−14.934		150.64	C
ATOM	10395	OD1	ASP F	15	2.191	11.418	−15.853		156.62	O
ATOM	10396	OD2	ASP F	15	2.794	10.697	−13.868		155.33	O1−
ATOM	10397	H	ASP F	15	6.148	13.103	−16.398		144.00	H
ATOM	10398	HA	ASP F	15	3.508	13.476	−16.105		144.65	H
ATOM	10399	HB2	ASP F	15	4.890	11.363	−15.754		152.39	H
ATOM	10400	HB3	ASP F	15	4.852	11.903	−14.260		152.39	H
ATOM	10401	N	THR F	16	3.269	14.937	−14.138		129.26	N
ATOM	10402	CA	THR F	16	3.188	15.852	−13.000		130.25	C
ATOM	10403	C	THR F	16	1.993	15.543	−12.102		131.07	C
ATOM	10404	O	THR F	16	0.939	15.126	−12.576		134.24	O
ATOM	10405	CB	THR F	16	3.080	17.323	−13.451		127.23	C
ATOM	10406	OG1	THR F	16	1.821	17.538	−14.099		133.36	O
ATOM	10407	CG2	THR F	16	4.217	17.692	−14.394		129.69	C
ATOM	10408	H	THR F	16	2.525	14.831	−14.556		135.11	H
ATOM	10409	HA	THR F	16	3.993	15.762	−12.467		136.30	H
ATOM	10410	HB	THR F	16	3.137	17.898	−12.672		132.67	H
ATOM	10411	HG1	THR F	16	1.758	18.338	−14.346		140.03	H
ATOM	10412	HG21	THR F	16	4.134	18.619	−14.667		135.62	H
ATOM	10413	HG22	THR F	16	5.070	17.570	−13.948		135.62	H
ATOM	10414	HG23	THR F	16	4.190	17.128	−15.183		135.62	H
ATOM	10415	N	HIS F	17	2.176	15.746	−10.799		127.94	N
ATOM	10416	CA	HIS F	17	1.086	15.654	−9.832		128.47	C
ATOM	10417	C	HIS F	17	1.094	16.890	−8.941		123.00	C
ATOM	10418	O	HIS F	17	2.112	17.220	−8.337		121.84	O
ATOM	10419	CB	HIS F	17	1.207	14.388	−8.985		130.82	C
ATOM	10420	CG	HIS F	17	1.084	13.122	−9.773		144.45	C
ATOM	10421	ND1	HIS F	17	2.129	12.592	−10.499		146.02	N
ATOM	10422	CD2	HIS F	17	0.037	12.283	−9.954		147.05	C
ATOM	10423	CE1	HIS F	17	1.733	11.479	−11.089		148.47	C
ATOM	10424	NE2	HIS F	17	0.467	11.269	−10.775		152.45	N
ATOM	10425	H	HIS F	17	2.935	15.943	−10.446		133.53	H
ATOM	10426	HA	HIS F	17	0.239	15.625	−10.304		134.16	H
ATOM	10427	HB2	HIS F	17	2.075	14.385	−8.551		136.99	H
ATOM	10428	HB3	HIS F	17	0.505	14.391	−8.316		136.99	H
ATOM	10429	HD1	HIS F	17	2.917	12.931	−10.557		155.22	H
ATOM	10430	HD2	HIS F	17	−0.813	12.374	−9.589		156.46	H
ATOM	10431	HE1	HIS F	17	2.255	10.936	−11.635		158.17	H
ATOM	10432	HE2	HIS F	17	−0.011	10.605	−11.042		162.94	H
ATOM	10433	N	SER F	18	−0.044	17.573	−8.879		117.98	N
ATOM	10434	CA	SER F	18	−0.177	18.794	−8.094		120.45	C
ATOM	10435	C	SER F	18	−1.131	18.561	−6.932		121.00	C
ATOM	10436	O	SER F	18	−2.266	18.124	−7.135		123.24	O
ATOM	10437	CB	SER F	18	−0.679	19.942	−8.971		122.54	C
ATOM	10438	OG	SER F	18	0.180	20.143	−10.082		130.00	O
ATOM	10439	H	SER F	18	−0.765	17.345	−9.289		121.57	H
ATOM	10440	HA	SER F	18	0.689	19.041	−7.734		124.54	H
ATOM	10441	HB2	SER F	18	−1.568	19.727	−9.294		127.05	H
ATOM	10442	HB3	SER F	18	−0.706	20.754	−8.442		127.05	H
ATOM	10443	HG	SER F	18	−0.107	20.775	−10.555		136.00	H
ATOM	10444	N	THR F	19	−0.665	18.867	−5.722		117.83	N
ATOM	10445	CA	THR F	19	−1.425	18.615	−4.501		118.00	C
ATOM	10446	C	THR F	19	−1.416	19.828	−3.570		116.45	C
ATOM	10447	O	THR F	19	−0.451	20.592	−3.537		114.39	O
ATOM	10448	CB	THR F	19	−0.853	17.389	−3.744		122.55	C
ATOM	10449	OG1	THR F	19	−0.964	16.223	−4.568		132.42	O
ATOM	10450	CG2	THR F	19	−1.601	17.142	−2.441		134.29	C
ATOM	10451	H	THR F	19	0.103	19.228	−5.581		121.39	H
ATOM	10452	HA	THR F	19	−2.346	18.421	−4.735		121.60	H
ATOM	10453	HB	THR F	19	0.081	17.548	−3.535		127.06	H
ATOM	10454	HG1	THR F	19	−0.656	15.555	−4.164		138.90	H
ATOM	10455	HG21	THR F	19	−1.226	16.372	−1.985		141.15	H
ATOM	10456	HG22	THR F	19	−1.526	17.917	−1.863		141.15	H
ATOM	10457	HG23	THR F	19	−2.539	16.975	−2.624		141.15	H
ATOM	10458	N	VAL F		20	−2.497	20.001	−2.817		115.56	N
ATOM	10459	CA	VAL F	20	−2.525	20.990	−1.749		113.89	C
ATOM	10460	C	VAL F	20	−3.255	20.430	−0.534		118.50	C
ATOM	10461	O	VAL F	20	−4.337	19.854	−0.660		118.47	O
ATOM	10462	CB	VAL F	20	−3.205	22.307	−2.177		112.52	C
ATOM	10463	CG1	VAL F	20	−2.985	23.371	−1.111		115.06	C
ATOM	10464	CG2	VAL F	20	−2.673	22.791	−3.519		117.29	C
ATOM	10465	H	VAL F		20	−3.228	19.557	−2.906		118.67	H
ATOM	10466	HA	VAL F		20	−1.615	21.194	−1.484		116.67	H
ATOM	10467	HB	VAL F	20	−4.160	22.159	−2.265		115.03	H
ATOM	10468	HG11	VAL F	20	−3.417	24.193	−1.393		118.07	H
ATOM	10469	HG12	VAL F		20	−3.369	23.065	−0.275		118.07	H
ATOM	10470	HG13	VAL F	20	−2.032	23.518	−1.005		118.07	H
ATOM	10471	HG21	VAL F	20	−3.121	23.618	−3.757		120.75	H
ATOM	10472	HG22	VAL F	20	−1.718	22.941	−3.444		120.75	H
ATOM	10473	HG23	VAL F	20	−2.850	22.114	−4.191		120.75	H
ATOM	10474	N	ASP F	21	−2.642	20.603	0.634		116.80	N
ATOM	10475	CA	ASP F	21	−3.255	20.265	1.914		117.58	C
ATOM	10476	C	ASP F	21	−3.462	21.536	2.730		117.01	C
ATOM	10477	O	ASP F	21	−2.575	22.388	2.787		115.14	O
ATOM	10478	CB	ASP F	21	−2.381	19.285	2.699		120.49	C
ATOM	10479	CG	ASP F	21	−2.160	17.976	1.967		126.72	C
ATOM	10480	OD1	ASP F	21	−3.111	17.480	1.325		129.73	O
ATOM	10481	OD2	ASP F	21	−1.031	17.446	2.035		137.52	O1−
ATOM	10482	H	ASP F	21	−1.848	20.923	0.712		120.16	H
ATOM	10483	HA	ASP F	21	−4.120	19.853	1.760		121.09	H
ATOM	10484	HB2	ASP F	21	−1.514	19.690	2.856		124.59	H
ATOM	10485	HB3	ASP F	21	−2.812	19.086	3.545		124.59	H
ATOM	10486	N	VAL F	22	−4.628	21.667	3.355		114.74	N
ATOM	10487	CA	VAL F	22	−4.883	22.786	4.259		114.88	C
ATOM	10488	C	VAL F	22	−5.074	22.258	5.674		115.42	C
ATOM	10489	O	VAL F	22	−5.919	21.397	5.914		116.90	O
ATOM	10490	CB	VAL F	22	−6.116	23.601	3.839		116.70	C
ATOM	10491	CG1	VAL F	22	−6.207	24.883	4.654		116.95	C
ATOM	10492	CG2	VAL F	22	−6.058	23.927	2.351		115.61	C
ATOM	10493	H	VAL F	22	−5.288	21.121	3.274		117.68	H
ATOM	10494	HA	VAL F	22	−4.114	23.378	4.257		117.85	H
ATOM	10495	HB	VAL F	22	−6.916	23.078	4.004		120.04	H
ATOM	10496	HG11	VAL F	22	−6.991	25.380	4.373		120.34	H
ATOM	10497	HG12	VAL F	22	−6.280	24.654	5.594		120.34	H
ATOM	10498	HG13	VAL F	22	−5.408	25.411	4.503		120.34	H
ATOM	10499	HG21	VAL F	22	−6.845	24.441	2.110		118.74	H
ATOM	10500	HG22	VAL F	22	−5.257	24.445	2.172		118.74	H
ATOM	10501	HG23	VAL F	2	−6.036	23.099	1.847		118.74	H
ATOM	10502	N	ASP F	23	−4.271	22.776	6.598		119.93	N
ATOM	10503	CA	ASP F	23	−4.308	22.361	7.994		118.92	C
ATOM	10504	C	ASP F	23	−4.743	23.509	8.899		120.49	C
ATOM	10505	O	ASP F	23	−4.200	24.612	8.815		116.14	O
ATOM	10506	CB	ASP F	23	−2.935	21.862	8.448		123.31	C
ATOM	10507	CG	ASP F	23	−2.429	20.687	7.628		132.67	C
ATOM	10508	OD1	ASP F	23	−3.251	19.964	7.023		126.04	O
ATOM	10509	OD2	ASP F	23	−1.196	20.485	7.601		134.54	O1−
ATOM	10510	H	ASP F	23	−3.684	23.383	6.436		123.92	H
ATOM	10511	HA	ASP F	23	−4.945	21.636	8.096		122.70	H
ATOM	10512	HB2	ASP F	23	−2.293	22.584	8.363		127.97	H
ATOM	10513	HB3	ASP F	23	−2.993	21.577	9.373		127.97	H
ATOM	10514	N	LEU F	24	−5.720	23.238	9.758		117.08	N
ATOM	10515	CA	LEU F	24	−6.114	24.167	10.813		121.44	C
ATOM	10516	C	LEU F	24	−5.627	23.618	12.149		125.10	C
ATOM	10517	O	LEU F	24	−6.105	22.581	12.603		124.75	O
ATOM	10518	CB	LEU F	24	−7.631	24.360	10.835		123.19	C
ATOM	10519	CG	LEU F	24	−8.183	25.284	11.926		126.52	C
ATOM	10520	CD1	LEU F	24	−7.713	26.717	11.715		125.95	C
ATOM	10521	CD2	LEU F	24	−9.702	25.220	11.967		124.61	C
ATOM	10522	H	LEU F	24	−6.177	22.510	9.751		120.50	H
ATOM	10523	HA	LEU F	24	−5.695	25.028	10.662		125.72	H
ATOM	10524	HB2	LEU F	24	−7.903	24.729	9.980		127.83	H
ATOM	10525	HB3	LEU F	24	−8.046	23.492	10.956		127.83	H
ATOM	10526	HG	LEU F	24	−7.850	24.986	12.787		131.82	H
ATOM	10527	HD11	LEU F	24	−8.078	27.275	12.419		131.14	H
ATOM	10528	HD12	LEU F	24	−6.743	26.738	11.745		131.14	H
ATOM	10529	HD13	LEU F	24	−8.025	27.027	10.851		131.14	H
ATOM	10530	HD21	LEU F	24	−10.024	25.813	12.664		129.53	H
ATOM	10531	HD22	LEU F	24	−10.052	25.499	11.107		129.53	H
ATOM	10532	HD23	LEU F	24	−9.974	24.308	12.156		129.53	H
ATOM	10533	N	ASP F	25	−4.675	24.310	12.767		121.21	N
ATOM	10534	CA	ASP F	25	−4.059	23.837	14.002		125.53	C
ATOM	10535	C	ASP F	25	−3.507	22.423	13.815		128.79	C
ATOM	10536	O	ASP F	25	−3.845	21.506	14.564		130.42	O
ATOM	10537	CB	ASP F	25	−5.064	23.874	15.157		122.66	C
ATOM	10538	CG	ASP F	25	−5.581	25.275	15.433		125.89	C
ATOM	10539	OD1	ASP F	25	−4.835	26.240	15.169		127.08	O
ATOM	10540	OD2	ASP F	25	−6.731	25.415	15.905		128.60	O1−
ATOM	10541	H	ASP F	25	−4.366	25.063	12.489		125.45	H
ATOM	10542	HA	ASP F	25	−3.318	24.420	14.230		130.64	H
ATOM	10543	HB2	ASP F	25	−5.823	23.312	14.935		127.20	H
ATOM	10544	HB3	ASP F	25	−4.634	23.548	15.963		127.20	H
ATOM	10545	N	ASP F	26	−2.662	22.266	12.799		127.45	N
ATOM	10546	CA	ASP F	26	−2.002	20.994	12.492		136.24	C
ATOM	10547	C	ASP F	26	−2.989	19.837	12.303		134.78	C
ATOM	10548	O	ASP F	26	−2.632	18.668	12.463		143.46	O
ATOM	10549	CB	ASP F	26	−0.987	20.646	13.588		140.63	C
ATOM	10550	CG	ASP F	26	0.210	21.582	13.591		147.72	C
ATOM	10551	OD1	ASP F	26	1.038	21.493	12.657		156.36	O
ATOM	10552	OD2	ASP F	26	0.328	22.403	14.526		147.17	O1−
ATOM	10553	H	ASP F	26	−2.448	22.899	12.256		132.93	H
ATOM	10554	HA	ASP F	26	−1.511	21.095	11.662		143.49	H
ATOM	10555	HB2	ASP F	26	−1.421	20.710	14.453		148.76	H
ATOM	10556	HB3	ASP F	26	−0.663	19.743	13.445		148.76	H
ATOM	10557	N	SER F	27	−4.227	20.173	11.955		132.09	N
ATOM	10558	CA	SER F	27	−5.231	19.180	11.597		134.04	C
ATOM	10559	C	SER F	27	−5.743	19.470	10.195		127.53	C
ATOM	10560	O	SER F	27	−6.229	20.565	9.922		125.46	O
ATOM	10561	CB	SER F	27	−6.386	19.183	12.596		135.84	C
ATOM	10562	OG	SER F	27	−7.408	18.294	12.181		139.50	O
ATOM	10563	H	SER F	27	−4.513	20.984	11.919		138.51	H
ATOM	10564	HA	SER F	27	−4.827	18.298	11.600		140.85	H
ATOM	10565	HB2	SER F	27	−6.055	18.903	13.463		143.01	H
ATOM	10566	HB3	SER F	27	−6.752	20.080	12.654		143.01	H
ATOM	10567	HG	SER F	27	−8.039	18.302	12.736		147.40	H
ATOM	10568	N	GLN F	28	−5.626	18.486	9.309		127.54	N
ATOM	10569	CA	GLN F	28	−6.030	18.651	7.918		123.96	C
ATOM	10570	C	GLN F	28	−7.541	18.819	7.811		123.35	C
ATOM	10571	O	GLN F	28	−8.295	18.020	8.367		123.17	O
ATOM	10572	CB	GLN F	28	−5.567	17.450	7.091		127.17	C
ATOM	10573	CG	GLN F	28	−5.639	17.658	5.595		125.49	C
ATOM	10574	CD	GLN F	28	−5.293	16.399	4.820		129.69	C
ATOM	10575	OE1	GLN F	28	−4.307	16.362	4.086		131.67	O
ATOM	10576	NE2	GLN F	28	−6.104	15.361	4.984		133.72	N
ATOM	10577	H	GLN F	28	−5.312	17.706	9.491		133.05	H
ATOM	10578	HA	GLN F	28	−5.610	19.447	7.556		128.76	H
ATOM	10579	HB2	GLN F	28	−4.644	17.254	7.317		132.60	H
ATOM	10580	HB3	GLN F	28	−6.126	16.688	7.310		132.60	H
ATOM	10581	HG2	GLN F	28	−6.540	17.922	5.355		130.58	H
ATOM	10582	HG3	GLN F	28	−5.009	18.351	5.341		130.58	H
ATOM	10583	HE21	GLN F	28	−5.950	14.625	4.566		140.46	H
ATOM	10584	HE22	GLN F	28	−6.783	15.424	5.508		140.46	H
ATOM	10585	N	ILE F	29	−7.974	19.862	7.102		118.13	N
ATOM	10586	CA	ILE F	29	−9.397	20.159	6.940		118.44	C
ATOM	10587	C	ILE F	29	−9.830	20.136	5.472		117.32	C
ATOM	10588	O	ILE F	29	−11.008	19.952	5.170		115.77	O
ATOM	10589	CB	ILE F	29	−9.757	21.539	7.544		116.85	C
ATOM	10590	CG1	ILE F	29	−8.943	22.655	6.879		118.54	C
ATOM	10591	CG2	ILE F	29	−9.505	21.533	9.044		121.09	C
ATOM	10592	CD1	ILE F	29	−9.442	24.060	7.198		116.42	C
ATOM	10593	H	ILE F	29	−7.456	20.418	6.700		121.76	H
ATOM	10594	HA	ILE F	29	−9.912	19.486	7.411		122.13	H
ATOM	10595	HB	ILE F	29	−10.699	21.708	7.389		120.22	H
ATOM	10596	HG12	ILE F	29	−8.024	22.592	7.181		122.25	H
ATOM	10597	HG13	ILE F	29	−8.982	22.538	5.917		122.25	H
ATOM	10598	HG21	ILE F	29	−9.735	22.404	9.405		125.31	H
ATOM	10599	HG22	ILE F	29	−10.056	20.848	9.454		125.31	H
ATOM	10600	HG23	ILE F	29	−8.568	21.345	9.206		125.31	H
ATOM	10601	HD11	ILE F	29	−8.879	24.705	6.742		119.71	H
ATOM	10602	HD12	ILE F	29	−10.358	24.147	6.891		119.71	H
ATOM	10603	HD13	ILE F	29	−9.399	24.201	8.156		119.71	H
ATOM	10604	N	ILE F	30	−8.874	20.338	4.571		118.05	N
ATOM	10605	CA	ILE F	30	−9.146	20.395	3.137		116.43	C
ATOM	10606	C	ILE F	30	−7.997	19.753	2.372		117.64	C
ATOM	10607	O	ILE F	30	−6.847	19.815	2.805		116.22	O
ATOM	10608	CB	ILE F	30	−9.324	21.855	2.635		116.66	C
ATOM	10609	CG1	ILE F	30	−10.499	22.548	3.327		119.53	C
ATOM	10610	CG2	ILE F	30	−9.533	21.893	1.120		117.34	C
ATOM	10611	CD1	ILE F	30	−10.513	24.061	3.112		122.20	C
ATOM	10612	H	ILE F	30	−8.044	20.446	4.768		121.66	H
ATOM	10613	HA	ILE F	30	−9.959	19.902	2.943		119.72	H
ATOM	10614	HB	ILE F	30	−8.515	22.348	2.842		120.00	H
ATOM	10615	HG12	ILE F	30	−11.329	22.189	2.974		123.44	H
ATOM	10616	HG13	ILE F	30	−10.445	22.382	4.281		123.44	H
ATOM	10617	HG21	ILE F	30	−9.641	22.816	0.840		120.81	H
ATOM	10618	HG22	ILE F	30	−8.759	21.503	0.685		120.81	H
ATOM	10619	HG23	ILE F	30	−10.329	21.385	0.899		120.81	H
ATOM	10620	HD11	ILE F	30	−11.278	24.438	3.574		126.64	H
ATOM	10621	HD12	ILE F	30	−9.692	24.437	3.468		126.64	H
ATOM	10622	HD13	ILE F	30	−10.576	24.244	2.161		126.64	H
ATOM	10623	N	THR F	31	−8.312	19.148	1.231		118.54	N
ATOM	10624	CA	THR F	31	−7.291	18.625	0.330		118.58	C
ATOM	10625	C	THR F	31	−7.672	18.886	−1.126		120.44	C
ATOM	10626	O	THR F	31	−8.849	19.000	−1.466		119.16	O
ATOM	10627	CB	THR F	31	−7.064	17.111	0.539		120.21	C
ATOM	10628	OG1	THR F	31	−5.973	16.673	−0.278		130.33	O
ATOM	10629	CG2	THR F	31	−8.309	16.315	0.191		126.70	C
ATOM	10630	H	THR F	31	−9.117	19.028	0.954		122.25	H
ATOM	10631	HA	THR F	31	−6.453	19.080	0.507		122.30	H
ATOM	10632	HB	THR F	31	−6.850	16.947	1.471		124.26	H
ATOM	10633	HG1	THR F	31	−5.273	17.088	−0.070		136.39	H
ATOM	10634	HG21	THR F	31	−8.147	15.369	0.328		132.04	H
ATOM	10635	HG22	THR F	31	−9.048	16.594	0.753		132.04	H
ATOM	10636	HG23	THR F	31	−8.547	16.463	−0.738		132.04	H
ATOM	10637	N	PHE F	32	−6.655	18.973	−1.976		119.67	N
ATOM	10638	CA	PHE F	32	−6.820	19.291	−3.391		118.78	C
ATOM	10639	C	PHE F	32	−5.886	18.375	−4.181		119.20	C
ATOM	10640	O	PHE F	32	−4.713	18.254	−3.833		116.31	O
ATOM	10641	CB	PHE F	32	−6.511	20.772	−3.633		115.72	C
ATOM	10642	CG	PHE F	32	−6.536	21.186	−5.076		118.98	C
ATOM	10643	CD1	PHE F	32	−7.727	21.534	−5.696		119.61	C
ATOM	10644	CD2	PHE F	32	−5.362	21.262	−5.804		116.15	C
ATOM	10645	CE1	PHE F	32	−7.745	21.928	−7.026		120.12	C
ATOM	10646	CE2	PHE F	32	−5.374	21.660	−7.130		117.52	C
ATOM	10647	CZ	PHE F	32	−6.568	21.992	−7.741		120.04	C
ATOM	10648	H	PHE F	32	−5.835	18.848	−1.750		123.60	H
ATOM	10649	HA	PHE F	32	−7.734	19.114	−3.663		122.53	H
ATOM	10650	HB2	PHE F	32	−7.168	21.307	−3.162		118.87	H
ATOM	10651	HB3	PHE F	32	−5.625	20.964	−3.288		118.87	H
ATOM	10652	HD1	PHE F	32	−8.523	21.492	−5.217		123.54	H
ATOM	10653	HD2	PHE F	32	−4.555	21.039	−5.399		119.38	H
ATOM	10654	HE1	PHE F	32	−8.550	22.153	−7.433		124.14	H
ATOM	10655	HE2	PHE F	32	−4.579	21.699	−7.611		121.02	H
ATOM	10656	HZ	PHE F	32	−6.578	22.257	−8.632		124.04	H
ATOM	10657	N	ASP F	33	−6.405	17.714	−5.216		119.97	N
ATOM	10658	CA	ASP F	33	−5.646	16.676	−5.927		121.68	C
ATOM	10659	C	ASP F	33	−5.216	17.090	−7.332		127.22	C
ATOM	10660	O	ASP F	33	−4.852	16.243	−8.152		129.98	O
ATOM	10661	CB	ASP F	33	−6.465	15.379	−6.003		124.51	C
ATOM	10662	CG	ASP F	33	−7.686	15.488	−6.923		128.43	C
ATOM	10663	OD1	ASP F	33	−7.945	16.569	−7.497		123.84	O
ATOM	10664	OD2	ASP F	33	−8.402	14.475	−7.060		125.95	O1−
ATOM	10665	H	ASP F	33	−7.196	17.846	−5.528		123.96	H
ATOM	10666	HA	ASP F	33	−4.841	16.483	−5.421		126.01	H
ATOM	10667	HB2	ASP F	33	−5.899	14.669	−6.343		129.41	H
ATOM	10668	HB3	ASP F	33	−6.781	15.154	−5.114		129.41	H
ATOM	10669	N	GLY F	34	−5.262	18.390	−7.604		124.60	N
ATOM	10670	CA	GLY F	34	−4.859	18.922	−8.894		123.43	C
ATOM	10671	C	GLY F	34	−6.046	19.347	−9.735		123.46	C
ATOM	10672	O	GLY F	34	−5.911	20.193	−10.618		127.08	O
ATOM	10673	H	GLY F	34	−5.527	18.991	−7.048		129.52	H
ATOM	10674	HA2	GLY F	34	−4.284	19.692	−8.762		128.12	H
ATOM	10675	HA3	GLY F	34	−4.362	18.246	−9.382		128.12	H
ATOM	10676	N	LYS F	35	−7.206	18.754	−9.457		124.09	N
ATOM	10677	CA	LYS F	35	−8.438	19.056	−10.187		131.50	C
ATOM	10678	C	LYS F	35	−9.588	19.327	−9.223		123.95	C
ATOM	10679	O	LYS F	35	−10.257	20.354	−9.316		124.63	O
ATOM	10680	CB	LYS F	35	−8.813	17.902	−11.122		136.85	C
ATOM	10681	CG	LYS F	35	−9.995	18.210	−12.039		153.02	C
ATOM	10682	CD	LYS F	35	−10.999	17.062	−12.114		167.53	C
ATOM	10683	CE	LYS F	35	−10.483	15.894	−12.943		193.83	C
ATOM	10684	NZ	LYS F	35	−9.481	15.062	−12.222		102.515	N1+
ATOM	10685	H	LYS F	35	−7.308	18.164	−8.840		128.91	H
ATOM	10686	HA	LYS F	35	−8.302	19.851	−10.726		137.80	H
ATOM	10687	HB2	LYS F	35	−8.049	17.693	−11.683		144.22	H
ATOM	10688	HB3	LYS F	35	−9.048	17.128	−10.586		144.22	H
ATOM	10689	HG2	LYS F	35	−10.459	18.993	−11.704		163.63	H
ATOM	10690	HG3	LYS F	35	−9.664	18.378	−12.935		163.63	H
ATOM	10691	HD2	LYS F	35	−11.179	16.739	−11.218		181.03	H
ATOM	10692	HD3	LYS F	35	−11.818	17.383	−12.523		181.03	H
ATOM	10693	HE2	LYS F	35	−11.230	15.323	−13.181		112.519	H
ATOM	10694	HE3	LYS F	35	−10.062	16.239	−13.746		112.519	H
ATOM	10695	HZ1	LYS F	35	−9.843	14.724	−11.482		123.016	H
ATOM	10696	HZ2	LYS F	35	−9.209	14.394	−12.743		123.016	H
ATOM	10697	HZ3	LYS F	35	−8.778	15.559	−11.998		123.016	H
ATOM	10698	N	ASP F	36	−9.807	18.396	−8.299		124.43	N
ATOM	10699	CA	ASP F	36	−10.926	18.476	−7.367		125.36	C
ATOM	10700	C	ASP F	36	−10.472	18.842	−5.959		123.53	C
ATOM	10701	O	ASP F	36	−9.384	18.462	−5.523		120.70	O
ATOM	10702	CB	ASP F	36	−11.679	17.146	−7.340		130.39	C
ATOM	10703	CG	ASP F	36	−12.330	16.821	−8.671		138.61	C
ATOM	10704	OD1	ASP F	36	−12.966	17.723	−9.258		137.40	O
ATOM	10705	OD2	ASP F	36	−12.199	15.669	−9.134		142.12	O1−
ATOM	10706	H	ASP F	36	−9.314	17.699	−8.191		129.32	H
ATOM	10707	HA	ASP F	36	−11.541	19.162	−7.671		130.43	H
ATOM	10708	HB2	ASP F	36	−11.056	16.433	−7.128		136.46	H
ATOM	10709	HB3	ASP F	36	−12.376	17.189	−6.667		136.46	H
ATOM	10710	N	ILE F	37	−11.317	19.592	−5.262		122.26	N
ATOM	10711	CA	ILE F	37	−11.081	19.940	−3.868		119.23	C
ATOM	10712	C	ILE F	37	−12.106	19.217	−3.019		120.45	C
ATOM	10713	O	ILE F	37	−13.226	18.982	−3.467		115.18	O
ATOM	10714	CB	ILE F	37	−11.176	21.460	−3.636		119.93	C
ATOM	10715	CG1	ILE F	37	−10.676	21.821	−2.235		123.69	C
ATOM	10716	CG2	ILE F	37	−12.600	21.958	−3.851		119.45	C
ATOM	10717	CD1	ILE F	37	−10.392	23.301	−2.070		121.55	C
ATOM	10718	H	ILE F	37	−12.046	19.918	−5.581		126.71	H
ATOM	10719	HA	ILE F	37	−10.197	19.642	−3.604		123.08	H
ATOM	10720	HB	ILE F	37	−10.602	21.899	−4.283		123.92	H
ATOM	10721	HG12	ILE F	37	−11.351	21.572	−1.585		128.43	H
ATOM	10722	HG13	ILE F	37	−9.854	21.337	−2.060		128.43	H
ATOM	10723	HG21	ILE F	37	−12.625	22.916	−3.698		123.34	H
ATOM	10724	HG22	ILE F	37	−12.868	21.762	−4.762		123.34	H
ATOM	10725	HG23	ILE F	37	−13.190	21.507	−3.227		123.34	H
ATOM	10726	HD11	ILE F	37	−10.080	23.463	−1.166		125.86	H
ATOM	10727	HD12	ILE F	37	−9.710	23.564	−2.708		125.86	H
ATOM	10728	HD13	ILE F	37	−11.208	23.799	−2.233		125.86	H
ATOM	10729	N	ARG F	38	−11.738	18.858	−1.797		117.84	N
ATOM	10730	CA	ARG F	38	−12.697	18.217	−0.916		120.68	C
ATOM	10731	C	ARG F	38	−12.396	18.455	0.558		119.35	C
ATOM	10732	O	ARG F	38	−11.235	18.589	0.953		118.38	O
ATOM	10733	CB	ARG F	38	−12.754	16.714	−1.198		122.95	C
ATOM	10734	CG	ARG F	38	−11.423	16.000	−1.117		128.32	C
ATOM	10735	CD	ARG F	38	−11.562	14.534	−1.510		133.42	C
ATOM	10736	NE	ARG F	38	−10.260	13.892	−1.685		143.09	N
ATOM	10737	CZ	ARG F	38	−9.592	13.252	−0.728		144.56	C
ATOM	10738	NH1	ARG F	38	−10.092	13.147	0.498		141.53	N1+
ATOM	10739	NH2	ARG F	38	−8.414	12.710	−1.002		157.47	N
ATOM	10740	H	ARG F	38	−10.954	18.971	−1.461		121.40	H
ATOM	10741	HA	ARG F	38	−13.576	18.584	−1.098		124.81	H
ATOM	10742	HB2	ARG F	38	−13.348	16.301	−0.551		127.54	H
ATOM	10743	HB3	ARG F	38	−13.104	16.580	−2.092		127.54	H
ATOM	10744	HG2	ARG F	38	−10.795	16.421	−1.725		133.98	H
ATOM	10745	HG3	ARG F	38	−11.091	16.041	−0.207		133.98	H
ATOM	10746	HD2	ARG F	38	−12.041	14.060	−0.812		140.11	H
ATOM	10747	HD3	ARG F	38	−12.045	14.473	−2.349		140.11	H
ATOM	10748	HE	ARG F	38	−9.899	13.931	−2.465		151.71	H
ATOM	10749	HH11	ARG F	38	−10.856	13.497	0.682		149.84	H
ATOM	10750	HH12	ARG F	38	−9.651	12.730	1.107		149.84	H
ATOM	10751	HH21	ARG F	38	−8.085	12.773	−1.794		168.96	H
ATOM	10752	HH22	ARG F	38	−7.979	12.293	−0.388		168.96	H
ATOM	10753	N	PRO F	39	−13.454	18.510	1.378		118.43	N
ATOM	10754	CA	PRO F	39	−13.287	18.624	2.828		118.67	C
ATOM	10755	CF	PRO F	39	−12.741	17.328	3.420		121.97	C
ATOM	10756	O	PRO F	39	13.015	16.261	2.874		121.02	O
ATOM	10757	CB	PRO F	39	−14.706	18.905	3.320		122.75	C
ATOM	10758	CG	PRO F	39	−15.585	18.250	2.306		122.23	C
ATOM	10759	CD	PRO F	39	−14.875	18.401	0.993		122.99	C
ATOM	10760	HA	PRO F	39	−12.704	19.365	3.054		122.40	H
ATOM	10761	HB2	PRO F	39	−14.835	18.509	4.196		127.30	H
ATOM	10762	HB3	PRO F	39	−14.861	19.862	3.346		127.30	H
ATOM	10763	HG2	PRO F	39	−15.696	17.312	2.528		126.68	H
ATOM	10764	HG3	PRO F	39	−16.445	18.699	2.282		126.68	H
ATOM	10765	HD2	PRO F	39	−15.016	17.616	0.441		127.59	H
ATOM	10766	HD3	PRO F	39	−15.166	19.209	0.543		127.59	H
ATOM	10767	N	THR F	40	−11.976	17.424	4.505		117.56	N
ATOM	10768	CA	THR F	40	−11.433	16.245	5.182		119.85	C
ATOM	10769	C	THR F	40	−11.726	16.306	6.680		121.64	C
ATOM	10770	O	THR F	40	−11.068	15.646	7.482		125.05	O
ATOM	10771	CB	THR F	40	−9.914	16.121	4.970		122.38	C
ATOM	10772	OG1	THR F	40	−9.253	17.246	5.562		122.26	O
ATOM	10773	CG2	THR F	40	−9.581	16.061	3.486		126.29	C
ATOM	10774	H	THR F	40	−11.755	18.169	4.874		121.07	H
ATOM	10775	HA	THR F	40	−11.855	15.449	4.823		123.82	H
ATOM	10776	HB	THR F	40	−9.596	15.305	5.387		126.85	H
ATOM	10777	HG1	THR F	40	−8.423	17.183	5.449		126.71	H
ATOM	10778	HG21	THR F	40	−8.622	15.983	3.364		131.55	H
ATOM	10779	HG22	THR F	40	−10.014	15.294	3.080		131.55	H
ATOM	10780	HG23	THR F	40	−9.890	16.868	3.044		131.55	H
ATOM	10781	N	ILE F	41	−12.714	17.115	7.042		120.01	N
ATOM	10782	CA	ILE F	41	−13.138	17.273	8.426		120.07	C
ATOM	10783	C	ILE F	41	−14.638	17.573	8.393		121.37	C
ATOM	10784	O	ILE F	41	−15.103	18.248	7.473		119.23	O
ATOM	10785	CB	ILE F	41	−12.348	18.400	9.131		120.97	C
ATOM	10786	CG1	ILE F	41	−12.551	18.369	10.647		125.82	C
ATOM	10787	CG2	ILE F	41	−12.723	19.766	8.564		119.25	C
ATOM	10788	CD1	ILE F	41	−11.871	17.205	11.329		128.28	C
ATOM	10789	H	ILE F	41	−13.164	17.595	6.490		124.01	H
ATOM	10790	HA	ILE F	41	−12.997	16.444	8.909		124.09	H
ATOM	10791	HB	ILE F	41	−11.405	18.256	8.956		125.16	H
ATOM	10792	HG12	ILE F	41	−12.191	19.186	11.027		130.99	H
ATOM	10793	HG13	ILE F	41	−13.500	18.310	10.834		130.99	H
ATOM	10794	HG21	ILE F	41	−12.213	20.450	9.024		123.10	H
ATOM	10795	HG22	ILE F	41	−12.517	19.780	7.616		123.10	H
ATOM	10796	HG23	ILE F	41	−13.673	19.913	8.698		123.10	H
ATOM	10797	HD11	ILE F	41	−12.044	17.254	12.282		133.93	H
ATOM	10798	HD12	ILE F	41	−12.227	16.378	10.969		133.93	H
ATOM	10799	HD13	ILE F	41	−10.917	17.255	11.162		133.93	H
ATOM	10800	N	PRO F	42	−15.407	17.061	9.370		122.08	N
ATOM	10801	CA	PRO F	42	−16.864	17.242	9.291		125.38	C
ATOM	10802	C	PRO F	42	−17.359	18.688	9.171		123.43	C
ATOM	10803	O	PRO F	42	−18.349	18.910	8.474		122.02	O
ATOM	10804	CB	PRO F	42	−17.353	16.627	10.603		129.94	C
ATOM	10805	CG	PRO F	42	−16.363	15.564	10.893		128.27	C
ATOM	10806	CD	PRO F	42	−15.038	16.104	10.431		125.21	C
ATOM	10807	HA	PRO F	42	−17.220	16.726	8.551		130.46	H
ATOM	10808	HB2	PRO F	42	−17.354	17.299	11.302		135.92	H
ATOM	10809	HB3	PRO F	42	−18.239	16.251	10.481		135.92	H
ATOM	10810	HG2	PRO F	42	−16.346	15.387	11.846		133.93	H
ATOM	10811	HG3	PRO F	42	−16.594	14.761	10.400		133.93	H
ATOM	10812	HD2	PRO F	42	−14.588	16.563	11.158		130.25	H
ATOM	10813	HD3	PRO F	42	−14.490	15.391	10.067		130.25	H
ATOM	10814	N	PHE F	43	−16.709	19.651	9.818		123.12	N
ATOM	10815	CA	PHE F	43	−17.256	21.005	9.831		124.79	C
ATOM	10816	C	PHE F	43	−17.066	21.713	8.486		123.64	C
ATOM	10817	O	PHE F	43	−17.626	22.787	8.262		121.80	O
ATOM	10818	CB	PHE F	43	−16.650	21.828	10.981		127.53	C
ATOM	10819	CG	PHE F	43	−15.249	22.323	10.736		122.90	C
ATOM	10820	CD1	PHE F	43	−15.021	23.465	9.986		124.94	C
ATOM	10821	CD2	PHE F	43	−14.165	21.676	11.301		125.76	C
ATOM	10822	CE1	PHE F	43	−13.736	23.932	9.777		125.31	C
ATOM	10823	CE2	PHE F	43	−12.876	22.141	11.097		125.44	C
ATOM	10824	CZ	PHE F	43	−12.663	23.270	10.336		123.75	C
ATOM	10825	H	PHE F	43	−15.970	19.552	10.246		127.75	H
ATOM	10826	HA	PHE F	43	−18.211	20.945	9.992		129.75	H
ATOM	10827	HB2	PHE F	43	−17.212	22.604	11.136		133.04	H
ATOM	10828	HB3	PHE F	43	−16.630	21.277	11.779		133.04	H
ATOM	10829	HD1	PHE F	43	−15.740	23.916	9.606		129.93	H
ATOM	10830	HD2	PHE F	43	−14.302	20.913	11.816		130.91	H
ATOM	10831	HE1	PHE F	43	−13.595	24.694	9.263		130.37	H
ATOM	10832	HE2	PHE F	43	−12.154	21.691	11.473		130.53	H
ATOM	10833	HZ	PHE F	43	−11.798	23.582	10.195		128.50	H
ATOM	10834	N	MET F	44	−16.306	21.100	7.584		122.56	N
ATOM	10835	CA	MET F	44	−16.106	21.657	6.248		122.07	C
ATOM	10836	C	MET F	44	−17.100	21.090	5.233		125.90	C
ATOM	10837	O	MET F	44	−17.186	21.573	4.099		124.02	O
ATOM	10838	CB	MET F	44	−14.672	21.401	5.776		123.53	C
ATOM	10839	CG	MET F	44	−13.629	22.258	6.480		117.23	C
ATOM	10840	SD	MET F	44	−13.962	24.032	6.367		124.19	S
ATOM	10841	CE	MET F	44	−14.044	24.258	4.597		116.78	C
ATOM	10842	H	MET F	44	−15.893	20.357	7.720		127.07	H
ATOM	10843	HA	MET F	44	−16.230	22.618	6.295		126.49	H
ATOM	10844	HB2	MET F	44	−14.451	20.471	5.940		128.24	H
ATOM	10845	HB3	MET F	44	−14.618	21.589	4.826		128.24	H
ATOM	10846	HG2	MET F	44	−13.609	22.019	7.420		120.67	H
ATOM	10847	HG3	MET F	44	−12.763	22.092	6.078		120.67	H
ATOM	10848	HE1	MET F	44	−14.222	25.193	4.407		120.13	H
ATOM	10849	HE2	MET F	44	−13.196	23.996	4.206		120.13	H
ATOM	10850	HE3	MET F	44	−14.758	23.706	4.242		120.13	H
ATOM	10851	N	ILE F	45	−17.856	20.074	5.637		123.53	N
ATOM	10852	CA	ILE F	45	−18.861	19.487	4.759		123.76	C
ATOM	10853	C	ILE F	45	−19.891	20.542	4.379		124.02	C
ATOM	10854	O	ILE F	45	−20.445	21.213	5.246		122.40	O
ATOM	10855	CB	ILE F	45	−19.570	18.284	5.427		124.34	C
ATOM	10856	CG1	ILE F	45	−18.585	17.130	5.642		126.48	C
ATOM	10857	CG2	ILE F	45	−20.768	17.817	4.596		127.47	C
ATOM	10858	CD1	ILE F	45	−18.072	16.491	4.363		131.71	C
ATOM	10859	H	ILE F	45	−17.806	19.707	6.413		128.23	H
ATOM	10860	HA	ILE F	45	−18.433	19.174	3.947		128.52	H
ATOM	10861	HB	ILE F	45	−19.896	18.569	6.295		129.20	H
ATOM	10862	HG12	ILE F	45	−17.818	17.464	6.132		131.78	H
ATOM	10863	HG13	ILE F	45	−19.027	16.438	6.159		131.78	H
ATOM	10864	HG21	ILE F	45	−21.188	17.065	5.043		132.97	H
ATOM	10865	HG22	ILE F	45	−21.400	18.549	4.516		132.97	H
ATOM	10866	HG23	ILE F	45	−20.458	17.550	3.717		132.97	H
ATOM	10867	HD11	ILE F	45	−17.459	15.775	4.593		138.05	H
ATOM	10868	HD12	ILE F	45	−18.824	16.136	3.864		138.05	H
ATOM	10869	HD13	ILE F	45	−17.613	17.164	3.837		138.05	H
ATOM	10870	N	GLY F	46	−20.129	20.692	3.080		123.90	N
ATOM	10871	CA	GLY F	46	−21.162	21.585	2.590		129.90	C
ATOM	10872	C	GLY F	46	−20.766	23.050	2.590		130.07	C
ATOM	10873	O	GLY F	46	−21.596	23.918	2.325		126.85	O
ATOM	10874	H	GLY F	46	−19.699	20.281	2.459		128.68	H
ATOM	10875	HA2	GLY F	46	−21.392	21.336	1.681		135.88	H
ATOM	10876	HA3	GLY F	46	−21.954	21.487	3.141		135.88	H
ATOM	10877	N	ASP F	47	−19.503	23.332	2.889		125.37	N
ATOM	10878	CA	ASP F	47	−19.003	24.700	2.842		122.15	C
ATOM	10879	C	ASP F	47	−19.092	25.225	1.417		119.48	C
ATOM	10880	O	ASP F	47	−18.683	24.548	0.479		123.63	O
ATOM	10881	CB	ASP F	47	−17.561	24.767	3.347		124.63	C
ATOM	10882	CG	ASP F	47	−16.915	26.115	3.090		124.37	C
ATOM	10883	OD1	ASP F	47	−17.287	27.091	3.769		127.78	O
ATOM	10884	OD2	ASP F	47	−16.032	26.196	2.212		127.63	O1−
ATOM	10885	H	ASP F	47	−18.915	22.749	3.122		130.44	H
ATOM	10886	HA	ASP F	47	−19.552	25.262	3.410		126.58	H
ATOM	10887	HB2	ASP F	47	−17.553	24.607	4.304		129.56	H
ATOM	10888	HB3	ASP F	47	−17.034	24.090	2.893		129.56	H
ATOM	10889	N	GLU F	48	−19.637	26.426	1.256		118.86	N
ATOM	10890	CA	GLU F	48	−19.825	27.004	−0.074		123.59	C
ATOM	10891	C	GLU F	48	−19.089	28.332	−0.224		118.84	C
ATOM	10892	O	GLU F	48	−19.333	29.078	−1.173		123.99	O
ATOM	10893	CB	GLU F	48	−21.321	27.185	−0.365		124.87	C
ATOM	10894	CG	GLU F	48	−22.059	28.030	0.656		125.98	C
ATOM	10895	CD	GLU F	48	−23.557	28.110	0.393		127.03	C
ATOM	10896	OE1	GLU F	48	−23.975	28.028	−0.781		127.18	O
ATOM	10897	OE2	GLU F	48	−24.316	28.257	1.368		124.72	O1−
ATOM	10898	H	GLU F	48	−19.907	26.928	1.900		122.64	H
ATOM	10899	HA	GLU F	48	−19.467	26.390	−0.734		128.31	H
ATOM	10900	HB2	GLU F	48	−21.420	27.614	−1.229		129.84	H
ATOM	10901	HB3	GLU F	48	−21.742	26.311	−0.384		129.84	H
ATOM	10902	HG2	GLU F	48	−21.930	27.643	1.536		131.18	H
ATOM	10903	HG3	GLU F	48	−21.702	28.932	0.635		131.18	H
ATOM	10904	N	ILE F	49	−18.176	28.615	0.701		121.84	N
ATOM	10905	CA	ILE F	49	−17.393	29.848	0.657		119.58	C
ATOM	10906	C	ILE F	49	−15.911	29.570	0.422		121.99	C
ATOM	10907	O	ILE F	49	−15.314	30.091	−0.521		118.32	O
ATOM	10908	CB	ILE F	49	−17.560	30.650	1.958		122.04	C
ATOM	10909	CG1	ILE F	49	−19.021	31.077	2.119		119.68	C
ATOM	10910	CG2	ILE F	49	−16.648	31.883	1.960		122.59	C
ATOM	10911	CD1	ILE F	49	−19.377	31.490	3.521		129.80	C
ATOM	10912	H	ILE F	49	−17.990	28.106	1.369		126.21	H
ATOM	10913	HA	ILE F	49	−17.714	30.397	−0.075		123.50	H
ATOM	10914	HB	ILE F	49	−17.317	30.082	2.707		126.45	H
ATOM	10915	HG12	ILE F	49	−19.192	31.832	1.534		123.61	H
ATOM	10916	HG13	ILE F	49	−19.594	30.334	1.874		123.61	H
ATOM	10917	HG21	ILE F	49	−16.775	32.368	2.791		127.11	H
ATOM	10918	HG22	ILE F	49	−15.726	31.594	1.883		127.11	H
ATOM	10919	HG23	ILE F	49	−16.882	32.449	1.208		127.11	H
ATOM	10920	HD11	ILE F	49	−20.312	31.747	3.546		135.76	H
ATOM	10921	HD12	ILE F	49	−19.222	30.743	4.119		135.76	H
ATOM	10922	HD13	ILE F	49	−18.820	32.242	3.779		135.76	H
ATOM	10923	N	PHE F	50	−15.317	28.749	1.279		114.92	N
ATOM	10924	CA	PHE F	50	−13.876	28.544	1.238		118.72	C
ATOM	10925	C	PHE F	50	−13.449	27.474	0.235		115.47	C
ATOM	10926	O	PHE F	50	−12.438	27.643	−0.442		115.17	O
ATOM	10927	CB	PHE F	50	−13.374	28.203	2.637		114.79	C
ATOM	10928	CG	PHE F	50	−13.688	29.267	3.644		120.85	C
ATOM	10929	CD1	PHE F	50	−12.912	30.413	3.720		123.04	C
ATOM	10930	CD2	PHE F	50	−14.778	29.144	4.488		121.71	C
ATOM	10931	CE1	PHEF	50	−13.206	31.407	4.633		121.89	C
ATOM	10932	CE2	PHE F		50	−15.074	30.134	5.408		121.18	C
ATOM	10933	CZ	PHE F	50	−14.288	31.268	5.475		119.57	C
ATOM	10934	H	PHE F		50	−15.724	28.301	1.890		117.90	H
ATOM	10935	HA	PHE F	50	−13.454	29.376	0.972		122.46	H
ATOM	10936	HB2	PHE F	50	−13.794	27.379	2.930		117.74	H
ATOM	10937	HB3	PHE F	50	−12.411	28.092	2.608		117.74	H
ATOM	10938	HD1	PHE F	50	−12.181	30.512	3.153		127.65	H
ATOM	10939	HD2	PHE F		50	−15.310	28.383	4.445		126.06	H
ATOM	10940	HE1	PHE F	50	−12.674	32.169	4.681		126.27	H
ATOM	10941	HE2	PHE F	50	−15.805	30.039	5.975		125.42	H
ATOM	10942	HZ	PHE F	50	−14.486	31.934	6.094		123.49	H
ATOM	10943	N	LEU F	51	−14.215	26.389	0.130		115.59	N
ATOM	10944	CA	LEU F	51	−13.877	25.314	−0.803		116.84	C
ATOM	10945	C	LEU F	51	−13.816	25.809	−2.251		114.18	C
ATOM	10946	O	LEU F	51	−12.842	25.549	−2.949		117.50	O
ATOM	10947	CB	LEU F	51	−14.878	24.157	−0.695		116.15	C
ATOM	10948	CG	LEU F	51	−14.747	23.235	0.521		123.56	C
ATOM	10949	CD1	LEU F	51	−15.930	22.279	0.591		125.39	C
ATOM	10950	CD2	LEU F	51	−13.442	22.452	0.490		118.07	C
ATOM	10951	H	LEU F	51	−14.931	26.251	0.585		118.71	H
ATOM	10952	HA	LEU F	51	−13.000	24.967	−0.573		120.21	H
ATOM	10953	HB2	LEU F	51	−15.772	24.533	−0.673		119.38	H
ATOM	10954	HB3	LEU F	51	−14.785	23.603	−1.485		119.38	H
ATOM	10955	HG	LEU F	51	−14.751	23.775	1.327		128.27	H
ATOM	10956	HD11	LEU F	51	−15.826	21.705	1.367		130.46	H
ATOM	10957	HD12	LEU F	51	−16.748	22.794	0.667		130.46	H
ATOM	10958	HD13	LEU F	51	−15.950	21.742	−0.217		130.46	H
ATOM	10959	HD21	LEU F	51	−13.398	21.882	1.274		121.69	H
ATOM	10960	HD22	LEU F	51	−13.418	21.911	−0.314		121.69	H
ATOM	10961	HD23	LEU F	51	−12.700	23.076	0.492		121.69	H
ATOM	10962	N	PRO F	52	−14.858	26.512	−2.718		115.74	N
ATOM	10963	CA	PRO F	52	−14.770	27.012	−4.094		116.28	C
ATOM	10964	C	PRO F	52	−13.685	28.072	−4.276		116.85	C
ATOM	10965	O	PRO F	52	−13.036	28.106	−5.322		115.38	O
ATOM	10966	CB	PRO F	52	−16.167	27.601	−4.350		119.09	C
ATOM	10967	CG	PRO F	52	−16.760	27.811	−3.003		120.50	C
ATOM	10968	CD	PRO F	52	−16.194	26.736	−2.139		120.80	C
ATOM	10969	HA	PRO F	52	−14.611	26.279	−4.710		119.54	H
ATOM	10970	HB2	PRO F	52	−16.084	28.443	−4.822		122.91	H
ATOM	10971	HB3	PRO F	52	−16.697	26.971	−4.862		122.91	H
ATOM	10972	HG2	PRO F	52	−16.507	28.686	−2.669		124.59	H
ATOM	10973	HG3	PRO F	52	−17.725	27.732	−3.057		124.59	H
ATOM	10974	HD2	PRO F	52	−16.119	27.042	−1.222		124.96	H
ATOM	10975	HD3	PRO F	52	−16.731	25.930	−2.204		124.96	H
ATOM	10976	N	PHE F	53	−13.485	28.921	−3.273		115.61	N
ATOM	10977	CA	PHE F	53	−12.478	29.970	−3.374		115.34	C
ATOM	10978	C	PHE F	53	−11.083	29.361	−3.477		114.81	C
ATOM	10979	O	PHE F	53	−10.293	29.756	−4.334		115.50	O
ATOM	10980	CB	PHE F	53	−12.555	30.922	−2.180		115.16	C
ATOM	10981	CG	PHE F	53	−11.510	32.002	−2.204		115.82	C
ATOM	10982	CD1	PHE F	53	−11.679	33.131	−2.989		115.97	C
ATOM	10983	CD2	PHE F	53	−10.356	31.885	−1.448		115.98	C
ATOM	10984	CE1	PHE F	53	−10.719	34.123	−3.016		118.86	C
ATOM	10985	CE2	PHE F	53	−9.392	32.879	−1.470		113.90	C
ATOM	10986	CZ	PHE F	53	−9.574	33.995	−2.256		113.75	C
ATOM	10987	H	PHE F	53	−13.916	28.910	−2.528		118.73	H
ATOM	10988	HA	PHE F	53	−12.640	30.486	−4.179		118.41	H
ATOM	10989	HB2	PHE F	53	−13.425	31.350	−2.176		118.19	H
ATOM	10990	HB3	PHE F	53	−12.436	30.411	−1.364		118.19	H
ATOM	10991	HD1	PHE F	53	−12.448	33.222	−3.504		119.16	H
ATOM	10992	HD2	PHE F	53	−10.229	31.133	−0.916		119.17	H
ATOM	10993	HE1	PHE F	53	−10.844	34.877	−3.546		122.64	H
ATOM	10994	HE2	PHE F	53	−8.620	32.791	−0.958		116.68	H
ATOM	10995	HZ	PHE F	53	−8.927	34.664	−2.272		116.50	H
ATOM	10996	N	TYR F	54	−10.790	28.389	−2.616		113.52	N
ATOM	10997	CA	TYR F	54	−9.500	27.707	−2.649		113.81	C
ATOM	10998	C	TYR F	54	−9.324	26.904	−3.935		113.72	C
ATOM	10999	O	TYR F	54	−8.222	26.831	−4.473		112.92	O
ATOM	11000	CB	TYR F	54	−9.338	26.783	−1.436		112.43	C
ATOM	11001	CG	TYR F	54	−9.215	27.502	−0.107		113.97	C
ATOM	11002	CD1	TYR F	54	−8.682	28.785	−0.029		115.04	C
ATOM	11003	CD2	TYR F	54	−9.637	26.899	1.070		114.73	C
ATOM	11004	CE1	TYR F	54	−8.575	29.442	1.182		113.01	C
ATOM	11005	CE2	TYR F	54	−9.531	27.545	2.282		113.82	C
ATOM	11006	CZ	TYR F	54	−9.002	28.814	2.333		114.13	C
ATOM	11007	OH	TYR F	54	−8.901	29.461	3.537		113.26	O
ATOM	11008	H	TYR F	54	−11.322	28.106	−2.003		116.22	H
ATOM	11009	HA	TYR F	54	−8.793	28.371	−2.614		116.57	H
ATOM	11010	HB2	TYR F	54	−10.112	26.201	−1.384		114.92	H
ATOM	11011	HB3	TYR F	54	−8.536	26.250	−1.557		114.92	H
ATOM	11012	HD1	TYR F	54	−8.395	29.208	−0.805		118.05	H
ATOM	11013	HD2	TYR F	54	−9.996	26.041	1.039		117.67	H
ATOM	11014	HE1	TYR F	54	−8.217	30.299	1.221		115.61	H
ATOM	11015	HE2	TYR F	54	−9.820	27.127	3.061		116.58	H
ATOM	11016	HH	TYR F	54	−9.194	28.970	4.152		115.91	H
ATOM	11017	N	LYS F	55	−10.403	26.303	−4.429		113.00	N
ATOM	11018	CA	LYS F	55	−10.321	25.526	−5.661		115.12	C
ATOM	11019	C	LYS F	55	−9.743	26.382	−6.786		114.25	C
ATOM	11020	O	LYS F	55	−8.873	25.934	−7.535		115.64	O
ATOM	11021	CB	LYS F	55	−11.695	24.982	−6.060		117.19	C
ATOM	11022	CG	LYS F	55	−11.638	23.938	−7.159		118.78	C
ATOM	11023	CD	LYS F	55	−13.025	23.546	−7.643		122.88	C
ATOM	11024	CE	LYS F	55	−12.935	22.564	−8.795		127.95	C
ATOM	11025	NZ	LYS F	55	−14.263	22.302	−9.406		135.34	N1+
ATOM	11026	H	LYS F	55	−11.186	26.330	−4.075		115.60	H
ATOM	11027	HA	LYS F	55	−9.727	24.772	−5.522		118.15	H
ATOM	11028	HB2	LYS F	55	−12.108	24.574	−5.283		120.62	H
ATOM	11029	HB3	LYS F	55	−12.243	25.717	−6.376		120.62	H
ATOM	11030	HG2	LYS F	55	−11.145	24.296	−7.913		122.53	H
ATOM	11031	HG3	LYS F	55	−11.200	23.142	−6.820		122.53	H
ATOM	11032	HD2	LYS F	55	−13.512	23.124	−6.918		127.45	H
ATOM	11033	HD3	LYS F	55	−13.495	24.337	−7.950		127.45	H
ATOM	11034	HE2	LYS F	55	−12.354	22.929	−9.480		133.53	H
ATOM	11035	HE3	LYS F	55	−12.581	21.722	−8.469		133.53	H
ATOM	11036	HZ1	LYS F	55	−14.180	21.724	−10.078		142.41	H
ATOM	11037	HZ2	LYS F	55	−14.816	21.961	−8.798		142.41	H
ATOM	11038	HZ3	LYS F	55	−14.609	23.060	−9.719		142.41	H
ATOM	11039	N	ASN F	56	−10.210	27.622	−6.886		112.64	N
ATOM	11040	CA	ASN F	56	−9.713	28.541	−7.906		115.26	C
ATOM	11041	C	ASN F	56	−8.293	29.017	−7.618		116.59	C
ATOM	11042	O	ASN F	56	−7.447	29.059	−8.511		115.03	O
ATOM	11043	CB	ASN F	56	−10.640	29.751	−8.028		118.33	C
ATOM	11044	CG	ASN F	56	−11.983	29.397	−8.634		128.04	C
ATOM	11045	OD1	ASN F	56	−12.091	28.463	−9.428		130.73	O
ATOM	11046	ND2	ASN F	56	−13.016	30.147	−8.264		132.03	N
ATOM	11047	H	ASN F	56	−10.815	27.957	−6.376		115.17	H
ATOM	11048	HA	ASN F	56	−9.706	28.085	−8.762		118.31	H
ATOM	11049	HB2	ASN F	56	−10.797	30.119	−7.144		122.00	H
ATOM	11050	HB3	ASN F	56	−10.220	30.416	−8.595		122.00	H
ATOM	11051	HD21	ASN F	56	−13.799	29.986	−8.581		138.43	H
ATOM	11052	HD22	ASN F	56	−12.901	30.792	−7.708		138.43	H
ATOM	11053	N	VAL F	57	−8.039	29.391	−6.370		112.10	N
ATOM	11054	CA	VAL F	57	−6.714	29.855	−5.972		112.15	C
ATOM	11055	C	VAL F		57	−5.674	28.762	−6.181		112.63	C
ATOM	11056	O	VAL F	57	−4.603	29.015	−6.738		116.24	O
ATOM	11057	CB	VAL F	57	−6.708	30.312	−4.500		112.42	C
ATOM	11058	CG1	VAL F	57	−5.284	30.566	−4.000		113.82	C
ATOM	11059	CG2	VAL F	57	−7.555	31.571	−4.342		113.89	C
ATOM	11060	H	VAL F		57	−8.617	29.386	−5.733		114.52	H
ATOM	11061	HA	VAL F		57	−6.467	30.615	−6.522		114.57	H
ATOM	11062	HB	VAL F	57	−7.100	29.615	−3.951		114.90	H
ATOM	11063	HG11	VAL F	57	−5.321	30.851	−3.074		116.59	H
ATOM	11064	HG12	VAL F		57	−4.772	29.745	−4.074		116.59	H
ATOM	11065	HG13	VAL F	57	−4.878	31.260	−4.544		116.59	H
ATOM	11066	HG21	VAL F	57	−7.541	31.845	−3.412		116.67	H
ATOM	11067	HG22	VAL F	57	−7.184	32.272	−4.900		116.67	H
ATOM	11068	HG23	VAL F	57	−8.464	31.375	−4.617		116.67	H
ATOM	11069	N	PHE F	58	−5.994	27.548	−5.740		112.82	N
ATOM	11070	CA	PHE F	58	−5.062	26.430	−5.830		113.09	C
ATOM	11071	C	PHE F	58	−4.801	26.058	−7.285		114.82	C
ATOM	11072	O	PHE F	58	−3.660	25.848	−7.676		112.06	O
ATOM	11073	CB	PHE F	58	−5.588	25.207	−5.070		112.73	C
ATOM	11074	CG	PHE F	58	−5.695	25.402	−3.578		112.49	C
ATOM	11075	CD1	PHE F	58	−5.281	26.581	−2.974		112.83	C
ATOM	11076	CD2	PHE F	58	−6.213	24.396	−2.777		113.83	C
ATOM	11077	CE1	PHE F	58	−5.388	26.751	−1.603		113.49	C
ATOM	11078	CE2	PHE F	58	−6.322	24.566	−1.405		116.44	C
ATOM	11079	CZ	PHE F	58	−5.906	25.747	−0.821		111.02	C
ATOM	11080	H	PHE F	58	−6.749	27.346	−5.381		115.38	H
ATOM	11081	HA	PHE F	58	−4.217	26.690	−5.431		115.71	H
ATOM	11082	HB2	PHE F	58	−6.473	24.991	−5.403		115.28	H
ATOM	11083	HB3	PHE F	58	−4.988	24.461	−5.227		115.28	H
ATOM	11084	HD1	PHE F	58	−4.931	27.267	−3.496		115.39	H
ATOM	11085	HD2	PHE F	58	−6.497	23.600	−3.166		116.60	H
ATOM	11086	HE1	PHE F	58	−5.107	27.546	−1.211		116.19	H
ATOM	11087	HE2	PHE F	58	−6.672	23.884	−0.878		119.73	H
ATOM	11088	HZ	PHE F	58	−5.975	25.862	0.099		113.22	H
ATOM	11089	N	SER F	59	−5.853	25.970	−8.089		112.82	N
ATOM	11090	CA	SER F	59	−5.685	25.598	−9.486		116.28	C
ATOM	11091	C	SER F	59	−4.855	26.649	−10.229		118.53	C
ATOM	11092	O	SER F	59	−4.011	26.307	−11.056		115.62	O
ATOM	11093	CB	SER F	59	−7.046	25.406	−10.159		119.61	C
ATOM	11094	OG	SER F	59	−7.896	26.504	−9.896		129.67	O
ATOM	11095	H	SER F	59	−6.667	26.119	−7.853		115.39	H
ATOM	11096	HA	SER F	59	−5.208	24.754	−9.532		119.54	H
ATOM	11097	HB2	SER F	59	−6.917	25.329	−11.118		123.54	H
ATOM	11098	HB3	SER F	59	−7.458	24.598	−9.815		123.54	H
ATOM	11099	HG	SER F	59	−7.551	27.212	−10.189		135.60	H
ATOM	11100	N	GLU F	60	−5.070	27.925	−9.914		117.84	N
ATOM	11101	CA	GLU F	60	−4.311	29.000	−10.554		115.88	C
ATOM	11102	C	GLU F	60	−2.856	29.027	−10.090		114.19	C
ATOM	11103	O	GLU F	60	−1.958	29.374	−10.859		116.59	O
ATOM	11104	CB	GLU F	60	−4.966	30.356	−10.286		119.52	C
ATOM	11105	CG	GLU F	60	−6.207	30.607	−11.124		126.68	C
ATOM	11106	CD	GLU F	60	−5.906	30.696	−12.609		134.90	C
ATOM	11107	OE1	GLU F	60	−5.129	31.593	−13.010		137.82	O
ATOM	11108	OE2	GLU F	60	−6.442	29.866	−13.377		135.67	O1−
ATOM	11109	H	GLU F	60	−5.646	28.194	−9.335		121.40	H
ATOM	11110	HA	GLU F	60	−4.313	28.855	−11.513		119.05	H
ATOM	11111	HB2	GLU F	60	−5.223	30.400	−9.352		123.42	H
ATOM	11112	HB3	GLU F	60	−4.326	31.058	−10.485		123.42	H
ATOM	11113	HG2	GLU F	60	−6.833	29.877	−10.988		132.02	H
ATOM	11114	HG3	GLU F	60	−6.610	31.445	−10.849		132.02	H
ATOM	11115	N	PHE F	61	−2.630	28.671	−8.829		116.80	N
ATOM	11116	CA	PHE F	61	−1.278	28.576	−8.290		113.01	C
ATOM	11117	C	PHE F	61	−0.415	27.700	−9.188		115.28	C
ATOM	11118	O	PHE F	61	0.721	28.048	−9.504		114.04	O
ATOM	11119	CB	PHE F	61	−1.302	28.013	−6.866		112.89	C
ATOM	11120	CG	PHE F	61	0.067	27.780	−6.272		111.72	C
ATOM	11121	CD1	PHE F	61	0.710	26.560	−6.430		112.06	C
ATOM	11122	CD2	PHE F	61	0.698	28.775	−5.538		112.10	C
ATOM	11123	CE1	PHE F	61	1.968	26.342	−5.878		114.29	C
ATOM	11124	CE2	PHE F	61	1.954	28.563	−4.982		112.57	C
ATOM	11125	CZ	PHE F	61	2.589	27.347	−5.152		111.10	C
ATOM	11126	H	PHE F	61	−3.247	28.479	−8.262		120.16	H
ATOM	11127	HA	PHE F	61	−0.883	29.462	−8.260		115.61	H
ATOM	11128	HB2	PHE F	61	−1.771	28.638	−6.292		115.46	H
ATOM	11129	HB3	PHE F	61	−1.768	27.162	−6.876		115.46	H
ATOM	11130	HD1	PHE F	61	0.299	25.884	−6.917		114.47	H
ATOM	11131	HD2	PHE F	61	0.277	29.596	−5.421		114.52	H
ATOM	11132	HE1	PHE F	61	2.391	25.522	−5.994		117.15	H
ATOM	11133	HE2	PHE F	61	2.368	29.240	−4.496		115.08	H
ATOM	11134	HZ	PHE F	61	3.429	27.203	−4.781		113.32	H
ATOM	11135	N	PHE F	62	−0.962	26.564	−9.605		115.38	N
ATOM	11136	CA	PHE F	62	−0.203	25.622	−10.419		114.52	C
ATOM	11137	C	PHE F	62	−0.191	26.018	−11.891		114.12	C
ATOM	11138	O	PHE F	62	0.847	25.938	−12.546		117.38	O
ATOM	11139	CB	PHE F	62	−0.762	24.209	−10.254		117.80	C
ATOM	11140	CG	PHE F	62	−0.503	23.620	−8.899		118.12	C
ATOM	11141	CD1	PHE F	62	0.767	23.192	−8.550		117.73	C
ATOM	11142	CD2	PHE F	62	−1.521	23.503	−7.972		113.87	C
ATOM	11143	CE1	PHE F	62	1.015	22.657	−7.305		114.74	C
ATOM	11144	CE2	PHE F	62	−1.279	22.972	−6.723		116.22	C
ATOM	11145	CZ	PHE F	62	−0.008	22.548	−6.389		116.45	C
ATOM	11146	H	PHE F	62	−1.767	26.316	−9.432		118.46	H
ATOM	11147	HA	PHE F	62	0.715	25.614	−10.108		117.42	H
ATOM	11148	HB2	PHE F	62	−1.722	24.233	−10.389		121.36	H
ATOM	11149	HB3	PHE F	62	−0.350	23.630	−10.914		121.36	H
ATOM	11150	HD1	PHE F	62	1.461	23.267	−9.165		121.28	H
ATOM	11151	HD2	PHE F	62	−2.378	23.790	−8.191		116.64	H
ATOM	11152	HE1	PHE F	62	1.872	22.372	−7.082		117.69	H
ATOM	11153	HE2	PHE F	62	−1.972	22.897	−6.108		119.47	H
ATOM	11154	HZ	PHE F	62	0.155	22.185	−5.548		119.74	H
ATOM	11155	N	SER F	63	−1.332	26.448	−12.416		115.98	N
ATOM	11156	CA	SER F	63	−1.421	26.766	−13.841		118.60	C
ATOM	11157	C	SER F	63	−0.623	28.019	−14.201		116.33	C
ATOM	11158	O	SER F	63	−0.291	28.231	−15.362		119.99	O
ATOM	11159	CB	SER F	63	−2.885	26.932	−14.267		122.18	C
ATOM	11160	OG	SER F	63	−3.490	28.031	−13.617		124.58	O
ATOM	11161	H	SER F	63	−2.062	26.565	−11.977		119.18	H
ATOM	11162	HA	SER F	63	−1.050	26.026	−14.347		122.32	H
ATOM	11163	HB2	SER F	63	−2.918	27.076	−15.225		126.61	H
ATOM	11164	HB3	SER F	63	−3.372	26.125	−14.037		126.61	H
ATOM	11165	HG	SER F	63	−4.290	28.105	−13.863		129.50	H
ATOM	11166	N	LEU F	64	−0.302	28.840	−13.206		115.47	N
ATOM	11167	CA	LEU F	64	0.496	30.041	−13.437		115.54	C
ATOM	11168	C	LEU F	64	1.991	29.730	−13.469		118.63	C
ATOM	11169	O	LEU F	64	2.785	30.540	−13.943		113.90	O
ATOM	11170	CB	LEU F	64	0.224	31.088	−12.353		115.69	C
ATOM	11171	CG	LEU F	64	−1.059	31.911	−12.474		116.40	C
ATOM	11172	CD1	LEU F	64	−1.282	32.718	−11.207		117.92	C
ATOM	11173	CD2	LEU F	64	−0.993	32.831	−13.679		121.55	C
ATOM	11174	H	LEU F	64	−0.534	28.724	−12.386		118.57	H
ATOM	11175	HA	LEU F	64	0.250	30.424	−14.293		118.64	H
ATOM	11176	HB2	LEU F	64	0.190	30.632	−11.498		118.83	H
ATOM	11177	HB3	LEU F	64	0.964	31.715	−12.350		118.83	H
ATOM	11178	HG	LEU F	64	−1.813	31.312	−12.590		119.68	H
ATOM	11179	HD11	LEU F	64	−2.099	33.233	−11.301		121.51	H
ATOM	11180	HD12	LEU F	64	−1.359	32.110	−10.456		121.51	H
ATOM	11181	HD13	LEU F	64	−0.528	33.314	−11.076		121.51	H
ATOM	11182	HD21	LEU F	64	−1.817	33.340	−13.732		125.87	H
ATOM	11183	HD22	LEU F	64	−0.238	33.432	−13.576		125.87	H
ATOM	11184	HD23	LEU F	64	−0.882	32.295	−14.479		125.87	H
ATOM	11185	N	PHE F	65	2.371	28.568	−12.946		114.47	N
ATOM	11186	CA	PHE F	65	3.784	28.206	−12.848		114.00	C
ATOM	11187	C	PHE F	65	4.326	27.740	−14.195		119.33	C
ATOM	11188	O	PHE F	65	3.872	26.736	−14.741		118.05	O
ATOM	11189	CB	PHE F	65	3.987	27.113	−11.797		112.53	C
ATOM	11190	CG	PHE F	65	5.433	26.750	−11.565		113.60	C
ATOM	11191	CD1	PHE F	65	6.370	27.728	−11.278		113.02	C
ATOM	11192	CD2	PHE F	65	5.845	25.432	−11.616		113.09	C
ATOM	11193	CE1	PHE F	65	7.694	27.395	−11.059		115.49	C
ATOM	11194	CE2	PHE F	65	7.169	25.093	−11.392		115.62	C
ATOM	11195	CZ	PHE F	65	8.092	26.076	−11.117		116.41	C
ATOM	11196	H	PHE F	65	1.833	27.972	−12.641		117.36	H
ATOM	11197	HA	PHE F	65	4.292	28.985	−12.573		116.80	H
ATOM	11198	HB2	PHE F	65	3.619	27.419	−10.954		115.03	H
ATOM	11199	HB3	PHE F	65	3.523	26.312	−12.087		115.03	H
ATOM	11200	HD1	PHE F	65	6.108	28.619	−11.239		115.62	H
ATOM	11201	HD2	PHE F	65	5.225	24.764	−11.803		115.71	H
ATOM	11202	HE1	PHE F	65	8.316	28.061	−10.870		118.58	H
ATOM	11203	HE2	PHE F	65	7.436	24.202	−11.434		118.74	H
ATOM	11204	HZ	PHE F	65	8.982	25.851	−10.969		119.69	H
ATOM	11205	N	ARG F	66	5.282	28.493	−14.731		115.25	N
ATOM	11206	CA	ARG F	66	5.986	28.096	−15.943		117.61	C
ATOM	11207	C	ARG F	66	7.345	27.528	−15.594		125.02	C
ATOM	11208	O	ARG F	66	8.085	28.103	−14.797		125.04	O
ATOM	11209	CB	ARG F	66	6.142	29.273	−16.894		118.04	C
ATOM	11210	CG	ARG F	66	4.896	29.554	−17.694		122.17	C
ATOM	11211	CD	ARG F	66	4.516	30.995	−17.574		124.66	C
ATOM	11212	NE	ARG F	66	5.588	31.875	−18.023		126.85	N
ATOM	11213	CZ	ARG F	66	5.720	33.140	−17.643		126.45	C
ATOM	11214	NH1	ARG F	66	4.850	33.681	−16.797		125.82	N1+
ATOM	11215	NH2	ARG F	66	6.724	33.865	−18.107		129.31	N
ATOM	11216	H	ARG F	66	5.544	29.245	−14.407		118.30	H
ATOM	11217	HA	ARG F	66	5.476	27.406	−16.396		121.13	H
ATOM	11218	HB2	ARG F	66	6.352	30.068	−16.379		121.65	H
ATOM	11219	HB3	ARG F	66	6.860	29.082	−17.517		121.65	H
ATOM	11220	HG2	ARG F	66	5.060	29.356	−18.629		126.60	H
ATOM	11221	HG3	ARG F	66	4.165	29.014	−17.356		126.60	H
ATOM	11222	HD2	ARG F	66	3.734	31.165	−18.123		129.59	H
ATOM	11223	HD3	ARG F	66	4.325	31.199	−16.646		129.59	H
ATOM	11224	HE	ARG F	66	6.139	31.571	−18.609		132.21	H
ATOM	11225	HH11	ARG F	66	4.195	33.211	−16.495		130.99	H
ATOM	11226	HH12	ARG F	66	4.940	34.500	−16.552		130.99	H
ATOM	11227	HH21	ARG F	66	7.289	33.516	−18.654		135.18	H
ATOM	11228	HH22	ARG F	66	6.814	34.684	−17.861		135.18	H
ATOM	11229	N	ARG F	67	7.660	26.395	−16.206		121.33	N
ATOM	11230	CA	ARG F	67	8.865	25.653	−15.896		125.35	C
ATOM	11231	C	ARG F	67	9.889	25.840	−17.006		130.18	C
ATOM	11232	O	ARG F	67	9.701	26.664	−17.904		129.69	O
ATOM	11233	CB	ARG F	67	8.526	24.172	−15.705		122.56	C
ATOM	11234	CG	ARG F	67	7.327	23.950	−14.797		121.84	C
ATOM	11235	CD	ARG F	67	7.287	22.543	−14.225		123.91	C
ATOM	11236	NE	ARG F	67	7.381	21.509	−15.253		127.20	N
ATOM	11237	CZ	ARG F	67	6.343	20.966	−15.883		131.04	C
ATOM	11238	NH1	ARG F	67	5.103	21.355	−15.613		127.45	N1+
ATOM	11239	NH2	ARG F	67	6.548	20.027	−16.798		129.30	N
ATOM	11240	H	ARG F	67	7.178	26.030	−16.818		125.59	H
ATOM	11241	HA	ARG F	67	9.246	25.989	−15.069		130.42	H
ATOM	11242	HB2	ARG F	67	8.324	23.781	−16.570		127.07	H
ATOM	11243	HB3	ARG F	67	9.289	23.723	−15.309		127.07	H
ATOM	11244	HG2	ARG F	67	7.370	24.575	−14.056		126.21	H
ATOM	11245	HG3	ARG F	67	6.513	24.092	−15.306		126.21	H
ATOM	11246	HD2	ARG F	67	8.034	22.429	−13.617		128.69	H
ATOM	11247	HD3	ARG F	67	6.451	22.419	−13.751		128.69	H
ATOM	11248	HE	ARG F	67	8.166	21.230	−15.466		132.65	H
ATOM	11249	HH11	ARG F	67	4.962	21.962	−15.021		132.94	H
ATOM	11250	HH12	ARG F	67	4.440	20.998	−16.028		132.94	H
ATOM	11251	HH21	ARG F	67	7.349	19.771	−16.980		135.16	H
ATOM	11252	HH22	ARG F	67	5.880	19.676	−17.211		135.16	H
ATOM	11253	N	VAL F	68	10.975	25.085	−16.925		132.53	N
ATOM	11254	CA	VAL F	68	11.988	25.069	−17.970		134.51	C
ATOM	11255	C	VAL F	68	12.281	23.609	−18.307		138.41	C
ATOM	11256	O	VAL F	68	12.207	22.750	−17.429		136.57	O
ATOM	11257	CB	VAL F	68	13.276	25.800	−17.529		141.03	C
ATOM	11258	CG1	VAL F	68	13.813	25.221	−16.223		139.01	C
ATOM	11259	CG2	VAL F	68	14.334	25.746	−18.624		143.43	C
ATOM	11260	H	VAL F	68	11.152	24.564	−16.264		139.04	H
ATOM	11261	HA	VAL F	68	11.642	25.505	−18.763		141.42	H
ATOM	11262	HB	VAL F	68	13.063	26.733	−17.371		149.24	H
ATOM	11263	HG11	VAL F	68	14.619	25.699	−15.974		146.81	H
ATOM	11264	HG12	VAL F	68	13.140	25.323	−15.532		146.81	H
ATOM	11265	HG13	VAL F	68	14.014	24.280	−16.354		146.81	H
ATOM	11266	HG21	VAL F	68	15.128	26.213	−18.318		152.11	H
ATOM	11267	HG22	VAL F	68	14.547	24.819	−18.811		152.11	H
ATOM	11268	HG23	VAL F	68	13.985	26.174	−19.421		152.11	H
ATOM	11269	N	PRO F	69	12.585	23.312	−19.583		140.10	N
ATOM	11270	CA	PRO F	69	12.933	21.923	−19.904		143.70	C
ATOM	11271	C	PRO F	69	14.276	21.526	−19.307		146.21	C
ATOM	11272	O	PRO F	69	15.248	22.268	−19.453		149.34	O
ATOM	11273	CB	PRO F	69	12.994	21.915	−21.437		142.03	C
ATOM	11274	CG	PRO F	69	12.269	23.147	−21.865		144.28	C
ATOM	11275	CD	PRO F	69	12.538	24.147	−20.794		137.27	C
ATOM	11276	HA	PRO F	69	12.243	21.314	−19.599		152.45	H
ATOM	11277	HB2	PRO F	69	13.919	21.944	−21.728		150.44	H
ATOM	11278	HB3	PRO F	69	12.552	21.122	−21.777		150.44	H
ATOM	11279	HG2	PRO F	69	12.619	23.453	−22.716		153.14	H
ATOM	11280	HG3	PRO F	69	11.319	22.961	−21.930		153.14	H
ATOM	11281	HD2	PRO F	69	13.392	24.582	−20.941		144.72	H
ATOM	11282	HD3	PRO F	69	11.813	24.789	−20.737		144.72	H
ATOM	11283	N	THR F	70	14.325	20.373	−18.647		148.67	N
ATOM	11284	CA	THR F	70	15.550	19.908	−18.009		160.44	C
ATOM	11285	C	THR F	70	15.727	18.407	−18.178		159.62	C
ATOM	11286	O	THR F	70	14.758	17.671	−18.367		155.15	O
ATOM	11287	CB	THR F	70	15.565	20.240	−16.507		159.77	C
ATOM	11288	OG1	THR F	70	14.479	19.568	−15.855		158.31	O
ATOM	11289	CG2	THR F	70	15.441	21.742	−16.286		162.29	C
ATOM	11290	H	THR F	70	13.657	19.840	−18.554		158.41	H
ATOM	11291	HA	THR F	70	16.309	20.349	−18.422		172.53	H
ATOM	11292	HB	THR F	70	16.404	19.943	−16.121		171.73	H
ATOM	11293	HG1	THR F	70	14.482	19.746	−15.034		169.97	H
ATOM	11294	HG21	THR F	70	15.451	21.939	−15.336		174.75	H
ATOM	11295	HG22	THR F	70	16.182	22.201	−16.711		174.75	H
ATOM	11296	HG23	THR F	70	14.609	22.065	−16.666		174.75	H
ATOM	11297	N	SER F	71	16.978	17.966	−18.107		161.53	N
ATOM	11298	CA	SER F	71	17.303	16.549	−18.178		166.52	C
ATOM	11299	C	SER F	71	16.917	15.841	−16.883		161.49	C
ATOM	11300	O	SER F	71	16.835	14.613	−16.840		159.94	O
ATOM	11301	CB	SER F	71	18.795	16.361	−18.457		170.57	C
ATOM	11302	OG	SER F	71	19.580	17.021	−17.479		174.17	O
ATOM	11303	H	SER F	71	17.665	18.476	−18.016		173.84	H
ATOM	11304	HA	SER F	71	16.805	16.144	−18.905		179.82	H
ATOM	11305	HB2	SER F	71	19.002	15.414	−18.441		184.68	H
ATOM	11306	HB3	SER F	71	19.002	16.731	−19.330		184.68	H
ATOM	11307	HG	SER F	71	20.396	16.911	−17.642		189.01	H
ATOM	11308	N	THR F	72	16.682	16.626	−15.833		162.01	N
ATOM	11309	CA	THR F	72	16.339	16.091	−14.517		154.74	C
ATOM	11310	C	THR F	72	15.134	15.150	−14.598		149.84	C
ATOM	11311	O	THR F	72	14.027	15.588	−14.906		153.35	O
ATOM	11312	CB	THR F	72	16.026	17.225	−13.522		157.21	C
ATOM	11313	OG1	THR F	72	17.057	18.220	−13.583		159.71	O
ATOM	11314	CG2	THR F	72	15.929	16.683	−12.103		149.20	C
ATOM	11315	H	THR F	72	16.715	17.485	−15.859		174.41	H
ATOM	11316	HA	THR F	72	17.093	15.587	−14.173		165.69	H
ATOM	11317	HB	THR F	72	15.176	17.629	−13.753		168.66	H
ATOM	11318	HG1	THR F	72	16.890	18.840	−13.042		171.65	H
ATOM	11319	HG21	THR F	72	15.732	17.405	−11.485		159.04	H
ATOM	11320	HG22	THR F	72	15.223	16.021	−12.049		159.04	H
ATOM	11321	HG23	THR F	72	16.769	16.270	−11.848		159.04	H
ATOM	11322	N	PRO F	73	15.345	13.851	−14.327		147.67	N
ATOM	11323	CA	PRO F	73	14.252	12.884	−14.470		142.23	C
ATOM	11324	C	PRO F	73	13.246	12.910	−13.323		144.81	C
ATOM	11325	O	PRO F	73	12.230	12.217	−13.393		143.07	O
ATOM	11326	CB	PRO F	73	14.984	11.543	−14.503		143.10	C
ATOM	11327	CG	PRO F	73	16.189	11.769	−13.668		142.60	C
ATOM	11328	CD	PRO F	73	16.597	13.199	−13.901		144.19	C
ATOM	11329	HA	PRO F	73	13.788	13.019	−15.311		150.67	H
ATOM	11330	HB2	PRO F	73	14.422	10.851	−14.121		151.72	H
ATOM	11331	HB3	PRO F	73	15.231	11.325	−15.416		151.72	H
ATOM	11332	HG2	PRO F	73	15.967	11.627	−12.734		151.12	H
ATOM	11333	HG3	PRO F	73	16.894	11.164	−13.946		151.12	H
ATOM	11334	HD2	PRO F	73	16.923	13.596	−13.078		153.02	H
ATOM	11335	HD3	PRO F	73	17.261	13.249	−14.607		153.02	H
ATOM	11336	N	TYR F	74	13.524	13.683	−12.280		143.68	N
ATOM	11337	CA	TYR F	74	12.612	13.764	−11.146		136.00	C
ATOM	11338	C	TYR F	74	12.852	15.007	−10.302		134.98	C
ATOM	11339	O	TYR F	74	13.985	15.312	−9.931		137.75	O
ATOM	11340	CB	TYR F	74	12.740	12.518	−10.271		134.00	C
ATOM	11341	CG	TYR F	74	11.779	12.501	−9.107		133.28	C
ATOM	11342	CD1	TYR F	74	10.522	11.926	−9.231		137.86	C
ATOM	11343	CD2	TYR F	74	12.124	13.064	−7.884		131.82	C
ATOM	11344	CE1	TYR F	74	9.637	11.908	−8.173		140.32	C
ATOM	11345	CE2	TYR F	74	11.245	13.051	−6.819		128.53	C
ATOM	11346	CZ	TYR F	74	10.003	12.472	−6.969		135.36	C
ATOM	11347	OH	TYR F	74	9.120	12.456	−5.915		137.99	O
ATOM	11348	H	TYR F	74	14.230	14.169	−12.204		152.42	H
ATOM	11349	HA	TYR F	74	11.702	13.801	−11.479		143.20	H
ATOM	11350	HB2	TYR F	74	12.565	11.734	−10.814		140.80	H
ATOM	11351	HB3	TYR F	74	13.641	12.477	−9.913		140.80	H
ATOM	11352	HD1	TYR F	74	10.273	11.545	−10.042		145.43	H
ATOM	11353	HD2	TYR F	74	12.961	13.455	−7.781		138.18	H
ATOM	11354	HE1	TYR F	74	8.799	11.519	−8.272		148.39	H
ATOM	11355	HE2	TYR F	74	11.489	13.431	−6.006		134.24	H
ATOM	11356	HH	TYR F	74	9.464	12.829	−5.246		145.59	H
ATOM	11357	N	GLU F	75	11.767	15.712	−9.998		132.78	N
ATOM	11358	CA	GLU F	75	11.816	16.888	−9.141		125.81	C
ATOM	11359	C	GLU F	75	10.590	16.935	−8.235		129.12	C
ATOM	11360	O	GLU F	75	9.484	16.581	−8.649		130.51	O
ATOM	11361	CB	GLU F	75	11.892	18.167	−9.974		135.92	C
ATOM	11362	CG	GLU F	75	13.193	18.358	−10.729		138.70	C
ATOM	11363	CD	GLU F	75	13.265	19.711	−11.411		141.84	C
ATOM	11364	OE1	GLU F	75	12.460	19.955	−12.333		139.49	O
ATOM	11365	OE2	GLU F	75	14.120	20.535	−11.018		143.44	O1−
ATOM	11366	H	GLU F	75	10.977	15.524	−10.282		139.33	H
ATOM	11367	HA	GLU F	75	12.607	16.843	−8.581		130.97	H
ATOM	11368	HB2	GLU F	75	11.174	18.154	−10.626		143.10	H
ATOM	11369	HB3	GLU F	75	11.781	18.928	−9.383		143.10	H
ATOM	11370	HG2	GLU F	75	13.934	18.294	−10.107		146.44	H
ATOM	11371	HG3	GLU F	75	13.269	17.672	−11.411		146.44	H
ATOM	11372	N	ASP F	76	10.798	17.370	−6.998		127.11	N
ATOM	11373	CA	ASP F	76	9.716	17.527	−6.037		125.30	C
ATOM	11374	C	ASP F	76	9.802	18.922	−5.426		118.73	C
ATOM	11375	O	ASP F	76	10.778	19.253	−4.754		119.05	O
ATOM	11376	CB	ASP F	76	9.793	16.447	−4.956		125.98	C
ATOM	11377	CG	ASP F	76	8.511	16.323	−4.158		133.41	C
ATOM	11378	OD1	ASP F	76	7.419	16.365	−4.766		128.50	O
ATOM	11379	OD2	ASP F	76	8.596	16.176	−2.919		144.45	O1−
ATOM	11380	H	ASP F	76	11.571	17.585	−6.687		132.53	H
ATOM	11381	HA	ASP F	76	8.864	17.444	−6.493		130.36	H
ATOM	11382	HB2	ASP F	76	9.969	15.591	−5.377		131.18	H
ATOM	11383	HB3	ASP F	76	10.509	16.667	−4.340		131.18	H
ATOM	11384	N	LEU F	77	8.786	19.738	−5.689		115.80	N
ATOM	11385	CA	LEU F	77	8.767	21.135	−5.256		115.34	C
ATOM	11386	C	LEU F	77	7.693	21.357	−4.206		119.57	C
ATOM	11387	O	LEU F	77	6.536	20.990	−4.414		116.25	O
ATOM	11388	CB	LEU F	77	8.520	22.055	−6.447		113.25	C
ATOM	11389	CG	LEU F	77	9.510	21.914	−7.604		118.29	C
ATOM	11390	CD1	LEU F	77	8.906	22.436	−8.889		124.51	C
ATOM	11391	CD2	LEU F	77	10.790	22.653	−7.281		121.55	C
ATOM	11392	H	LEU F	77	8.083	19.504	−6.125		118.96	H
ATOM	11393	HA	LEU F	77	9.626	21.362	−4.868		118.41	H
ATOM	11394	HB2	LEU F	77	7.635	21.872	−6.798		115.90	H
ATOM	11395	HB3	LEU F	77	8.562	22.974	−6.138		115.90	H
ATOM	11396	HG	LEU F	77	9.724	20.976	−7.728		121.95	H
ATOM	11397	HD11	LEU F	77	9.553	22.336	−9.605		129.41	H
ATOM	11398	HD12	LEU F	77	8.106	21.927	−9.092		129.41	H
ATOM	11399	HD13	LEU F	77	8.682	23.373	−8.775		129.41	H
ATOM	11400	HD21	LEU F	77	11.407	22.554	−8.024		125.86	H
ATOM	11401	HD22	LEU F	77	10.587	23.591	−7.143		125.86	H
ATOM	11402	HD23	LEU F	77	11.178	22.276	−6.476		125.86	H
ATOM	11403	N	THR F	78	8.072	21.965	−3.086		113.26	N
ATOM	11404	CA	THR F	78	7.124	22.221	−2.009		115.50	C
ATOM	11405	C	THR F	78	7.129	23.689	−1.608		115.27	C
ATOM	11406	O	THR F	78	8.182	24.310	−1.481		115.66	O
ATOM	11407	CB	THR F	78	7.432	21.361	−0.771		115.80	C
ATOM	11408	OG1	THR F	78	7.512	19.982	−1.150		121.65	O
ATOM	11409	CG2	THR F	78	6.354	21.526	0.287		119.77	C
ATOM	11410	H	THR F	78	8.872	22.239	−2.925		115.91	H
ATOM	11411	HA	THR F	78	6.231	21.997	−2.315		118.60	H
ATOM	11412	HB	THR F	78	8.280	21.639	−0.389		118.96	H
ATOM	11413	HG1	THR F	78	8.122	19.875	−1.718		125.98	H
ATOM	11414	HG21	THR F	78	6.562	20.978	1.060		123.73	H
ATOM	11415	HG22	THR F	78	6.299	22.454	0.563		123.73	H
ATOM	11416	HG23	THR F	78	5.494	21.252	−0.071		123.73	H
ATOM	11417	N	TYR F	79	5.934	24.232	−1.417		114.59	N
ATOM	11418	CA	TYR F	79	5.771	25.580	−0.895		114.36	C
ATOM	11419	C	TYR F	79	4.795	25.527	0.268		113.77	C
ATOM	11420	O	TYR F	79	3.654	25.085	0.126		111.30	O
ATOM	11421	CB	TYR F	79	5.286	26.537	−1.984		115.36	C
ATOM	11422	CG	TYR F	79	4.973	27.937	−1.494		112.43	C
ATOM	11423	CD1	TYR F	79	5.935	28.706	−0.856		114.93	C
ATOM	11424	CD2	TYR F	79	3.715	28.493	−1.685		115.01	C
ATOM	11425	CE1	TYR F	79	5.651	29.988	−0.417		116.52	C
ATOM	11426	CE2	TYR F	79	3.424	29.768	−1.249		112.69	C
ATOM	11427	CZ	TYR F	79	4.392	30.510	−0.614		114.82	C
ATOM	11428	OH	TYR F	79	4.099	31.784	−0.184		118.09	O
ATOM	11429	H	TYR F	79	5.191	23.833	−1.585		117.51	H
ATOM	11430	HA	TYR F	79	6.624	25.901	−0.564		117.24	H
ATOM	11431	HB2	TYR F	79	5.975	26.611	−2.663		118.43	H
ATOM	11432	HB3	TYR F	79	4.477	26.175	−2.378		118.43	H
ATOM	11433	HD1	TYR F	79	6.785	28.354	−0.721		117.91	H
ATOM	11434	HD2	TYR F	79	3.056	27.995	−2.112		118.01	H
ATOM	11435	HE1	TYR F	79	6.305	30.491	0.012		119.83	H
ATOM	11436	HE2	TYR F	79	2.575	30.124	−1.383		115.23	H
ATOM	11437	HH	TYR F	79	4.774	32.127	0.179		121.71	H
ATOM	11438	N	PHE F	80	5.280	25.957	1.426		114.96	N
ATOM	11439	CA	PHE F	80	4.514	25.945	2.660		115.84	C
ATOM	11440	C	PHE F	80	4.224	27.377	3.071		115.28	C
ATOM	11441	O	PHE F	80	5.138	28.191	3.150		115.47	O
ATOM	11442	CB	PHE F	80	5.287	25.213	3.754		120.98	C
ATOM	11443	CG	PHE F	80	4.626	25.256	5.097		122.06	C
ATOM	11444	CD1	PHE F	80	3.607	24.372	5.411		122.52	C
ATOM	11445	CD2	PHE F	80	5.030	26.173	6.052		119.44	C
ATOM	11446	CE1	PHE F	80	3.000	24.406	6.653		124.51	C
ATOM	11447	CE2	PHE F	80	4.426	26.211	7.295		120.54	C
ATOM	11448	CZ	PHE F	80	3.412	25.328	7.596		120.28	C
ATOM	11449	H	PHE F	80	6.075	26.269	1.522		117.96	H
ATOM	11450	HA	PHE F	80	3.671	25.487	2.516		119.00	H
ATOM	11451	HB2	PHE F	80	5.381	24.282	3.500		125.17	H
ATOM	11452	HB3	PHE F	80	6.163	25.619	3.842		125.17	H
ATOM	11453	HD1	PHE F	80	3.327	23.749	4.780		127.02	H
ATOM	11454	HD2	PHE F	80	5.714	26.771	5.855		123.33	H
ATOM	11455	HE1	PHE F	80	2.316	23.809	6.854		129.42	H
ATOM	11456	HE2	PHE F	80	4.704	26.833	7.929		124.65	H
ATOM	11457	HZ	PHE F	80	3.005	25.353	8.432		124.33	H
ATOM	11458	N	TYR F	81	2.952	27.686	3.295		113.47	N
ATOM	11459	CA	TYR F	81	2.553	29.014	3.746		115.11	C
ATOM	11460	C	TYR F	81	1.595	28.918	4.926		117.28	C
ATOM	11461	O	TYR F	81	0.586	28.208	4.869		114.65	O
ATOM	11462	CB	TYR F	81	1.905	29.803	2.614		112.73	C
ATOM	11463	CG	TYR F	81	1.506	31.189	3.044		117.49	C
ATOM	11464	CD1	TYR F	81	2.430	32.225	3.046		116.62	C
ATOM	11465	CD2	TYR F	81	0.213	31.459	3.469		114.65	C
ATOM	11466	CE1	TYR F	81	2.073	33.496	3.451		119.10	C
ATOM	11467	CE2	TYR F	81	−0.152	32.725	3.879		118.37	C
ATOM	11468	CZ	TYR F	81	0.781	33.739	3.866		119.41	C
ATOM	11469	OH	TYR F	81	0.420	35.004	4.267		120.36	O
ATOM	11470	H	TYR F	81	2.295	27.140	3.193		116.17	H
ATOM	11471	HA	TYR F	81	3.341	29.499	4.038		118.13	H
ATOM	11472	HB2	TYR F	81	2.535	29.884	1.881		115.28	H
ATOM	11473	HB3	TYR F	81	1.107	29.337	2.318		115.28	H
ATOM	11474	HD1	TYR F	81	3.302	32.061	2.768		119.95	H
ATOM	11475	HD2	TYR F	81	−0.418	30.776	3.480		117.58	H
ATOM	11476	HE1	TYR F	81	2.700	34.182	3.444		122.92	H
ATOM	11477	HE2	TYR F	81	−1.023	32.894	4.157		122.05	H
ATOM	11478	HH	TYR F	81	−0.389	35.014	4.493		124.43	H
ATOM	11479	N	GLU F	82	1.910	29.648	5.991		115.52	N
ATOM	11480	CA	GLU F	82	1.145	29.563	7.224		115.50	C
ATOM	11481	C	GLU F	82	0.925	30.935	7.832		119.21	C
ATOM	11482	O	GLU F	82	1.858	31.731	7.929		116.31	O
ATOM	11483	CB	GLU F	82	1.865	28.661	8.228		118.78	C
ATOM	11484	CG	GLU F	82	1.115	28.456	9.537		121.18	C
ATOM	11485	CD	GLU F	82	1.954	27.739	10.577		128.40	C
ATOM	11486	OE1	GLU F	82	2.678	28.425	11.330		128.83	O
ATOM	11487	OE2	GLU F	82	1.893	26.492	10.637		129.39	O1−
ATOM	11488	H	GLU F	82	2.567	30.202	6.022		118.63	H
ATOM	11489	HA	GLU F	82	0.278	29.173	7.034		118.59	H
ATOM	11490	HB2	GLU F	82	1.996	27.789	7.824		122.54	H
ATOM	11491	HB3	GLU F	82	2.725	29.056	8.440		122.54	H
ATOM	11492	HG2	GLU F	82	0.864	29.321	9.897		125.42	H
ATOM	11493	HG3	GLU F	82	0.323	27.922	9.369		125.42	H
ATOM	11494	N	CYS F	83	−0.314	31.205	8.236		116.05	N
ATOM	11495	CA	CYS F	83	−0.618	32.408	8.996		114.60	C
ATOM	11496	C	CYS F	83	−1.077	31.989	10.386		117.53	C
ATOM	11497	O	CYS F	83	−1.688	30.932	10.562		119.01	O
ATOM	11498	CB	CYS F	83	−1.672	33.270	8.287		121.05	C
ATOM	11499	SG	CYS F	83	−3.338	32.591	8.159		120.77	S
ATOM	11500	H	CYS F	83	−0.996	30.705	8.082		119.26	H
ATOM	11501	HA	CYS F	83	0.189	32.937	9.092		117.52	H
ATOM	11502	HB2	CYS F	83	−1.742	34.112	8.763		125.26	H
ATOM	11503	HB3	CYS F	83	−1.363	33.440	7.383		125.26	H
ATOM	11504	N	ASP F	84	−0.746	32.815	11.370		113.89	N
ATOM	11505	CA	ASP F	84	−1.007	32.510	12.768		117.39	C
ATOM	11506	C	ASP F	84	−1.702	33.696	13.425		121.87	C
ATOM	11507	O	ASP F	84	−1.286	34.844	13.257		119.44	O
ATOM	11508	CB	ASP F	84	0.302	32.175	13.492		119.88	C
ATOM	11509	CG	ASP F	84	0.095	31.813	14.952		129.70	C
ATOM	11510	OD1	ASP F	84	−0.328	32.693	15.737		123.11	O
ATOM	11511	OD2	ASP F	84	0.378	30.651	15.318		131.40	O1−
ATOM	11512	H	ASP F	84	−0.361	33.574	11.250		116.67	H
ATOM	11513	HA	ASP F	84	−1.595	31.740	12.826		120.87	H
ATOM	11514	HB2	ASP F	84	0.721	31.418	13.053		123.86	H
ATOM	11515	HB3	ASP F	84	0.889	32.946	13.456		123.86	H
ATOM	11516	N	TYR F	85	−2.766	33.406	14.165		117.83	N
ATOM	11517	CA	TYR F	85	−3.500	34.426	14.897		120.90	C
ATOM	11518	C	TYR F	85	−3.523	34.050	16.370		121.48	C
ATOM	11519	O	TYR F	85	−4.217	33.118	16.776		122.77	O
ATOM	11520	CB	TYR F	85	−4.918	34.575	14.344		120.94	C
ATOM	11521	CG	TYR F	85	−5.590	35.873	14.726		119.46	C
ATOM	11522	CD1	TYR F	85	−5.044	37.093	14.351		123.95	C
ATOM	11523	CD2	TYR F	85	−6.781	35.880	15.443		124.58	C
ATOM	11524	CE1	TYR F	85	−5.652	38.284	14.690		121.09	C
ATOM	11525	CE2	TYR F	85	−7.401	37.068	15.784		125.21	C
ATOM	11526	CZ	TYR F	85	−6.831	38.266	15.402		124.37	C
ATOM	11527	OH	TYR F	85	−7.436	39.454	15.734		124.90	O
ATOM	11528	H	TYR F	85	−3.086	32.614	14.260		121.40	H
ATOM	11529	HA	TYR F	85	−3.045	35.278	14.806		125.08	H
ATOM	11530	HB2	TYR F	85	−4.881	34.535	13.375		125.13	H
ATOM	11531	HB3	TYR F	85	−5.463	33.848	14.683		125.13	H
ATOM	11532	HD1	TYR F	85	−4.248	37.108	13.870		128.73	H
ATOM	11533	HD2	TYR F	85	−7.165	35.073	15.699		129.50	H
ATOM	11534	HE1	TYR F	85	−5.272	39.093	14.434		125.31	H
ATOM	11535	HE2	TYR F	85	−8.196	37.059	16.266		130.25	H
ATOM	11536	HH	TYR F	85	−8.142	39.306	16.164		129.88	H
ATOM	11537	N	THR F	86	−2.739	34.777	17.158		120.16	N
ATOM	11538	CA	THR F	86	−2.580	34.497	18.577		123.51	C
ATOM	11539	C	THR F	86	−2.558	35.808	19.355		122.77	C
ATOM	11540	O	THR F	86	−1.775	36.704	19.040		122.32	O
ATOM	11541	CB	THR F	86	−1.280	33.708	18.847		127.41	C
ATOM	11542	OG1	THR F	86	−1.277	32.503	18.069		122.82	O
ATOM	11543	CG2	THR F	86	−1.153	33.353	20.320		124.65	C
ATOM	11544	H	THR F	86	−2.280	35.452	16.887		124.20	H
ATOM	11545	HA	THR F	86	−3.331	33.967	18.889		128.22	H
ATOM	11546	HB	THR F	86	−0.517	34.252	18.598		132.89	H
ATOM	11547	HG1	THR F	86	−1.322	32.690	17.251		127.38	H
ATOM	11548	HG21	THR F	86	−0.333	32.858	20.472		129.58	H
ATOM	11549	HG22	THR F	86	−1.138	34.161	20.856		129.58	H
ATOM	11550	HG23	THR F	86	−1.906	32.806	20.596		129.58	H
ATOM	11551	N	ASP F	87	−3.415	35.920	20.367		121.80	N
ATOM	11552	CA	ASP F	87	−3.493	37.140	21.166		121.76	C
ATOM	11553	C	ASP F	87	−3.709	38.351	20.255		125.94	C
ATOM	11554	O	ASP F	87	−3.058	39.382	20.404		124.45	O
ATOM	11555	CB	ASP F	87	−2.221	37.313	22.002		124.06	C
ATOM	11556	CG	ASP F	87	−2.336	38.433	23.021		125.87	C
ATOM	11557	OD1	ASP F	87	−3.451	38.663	23.533		126.46	O
ATOM	11558	OD2	ASP F	87	−1.309	39.082	23.305		127.96	O1−
ATOM	11559	H	ASP F	87	−3.962	35.304	20.612		126.15	H
ATOM	11560	HA	ASP F	87	−4.248	37.077	21.772		126.11	H
ATOM	11561	HB2	ASP F	87	−2.043	36.489	22.480		128.88	H
ATOM	11562	HB3	ASP F	87	−1.480	37.521	21.411		128.88	H
ATOM	11563	N	ASN F	88	−4.611	38.192	19.291		122.91	N
ATOM	11564	CA	ASN F	88	−4.971	39.255	18.351		124.97	C
ATOM	11565	C	ASN F	88	−3.803	39.741	17.489		123.23	C
ATOM	11566	O	ASN F	88	−3.880	40.805	16.877		124.47	O
ATOM	11567	CB	ASN F	88	−5.580	40.433	19.112		125.84	C
ATOM	11568	CG	ASN F	88	−6.788	40.027	19.930		136.58	C
ATOM	11569	OD1	ASN F	88	−6.720	39.928	21.155		144.27	O
ATOM	11570	ND2	ASN F	88	−7.905	39.783	19.253		140.67	N
ATOM	11571	H	ASN F	88	−5.040	37.459	19.157		127.49	H
ATOM	11572	HA	ASN F	88	−5.651	38.913	17.750		129.96	H
ATOM	11573	HB2	ASN F	88	−4.916	40.798	19.717		131.01	H
ATOM	11574	HB3	ASN F	88	−5.861	41.110	18.477		131.01	H
ATOM	11575	HD2	ASN F	88	−8.619	39.549	19.671		148.81	H
ATOM	11576	HD22	ASN F	88	−7.914	39.859	18.396		148.81	H
ATOM	11577	N	LYS F	89	−2.736	38.952	17.429		119.11	N
ATOM	11578	CA	LYS F	89	−1.563	39.305	16.639		123.78	C
ATOM	11579	C	LYS F	89	−1.421	38.394	15.422		122.87	C
ATOM	11580	O	LYS F	89	−1.475	37.167	15.537		122.29	O
ATOM	11581	CB	LYS F	89	−0.303	39.240	17.503		126.55	C
ATOM	11582	CG	LYS F	89	−0.226	40.350	18.549		132.53	C
ATOM	11583	CD	LYS F	89	0.900	40.113	19.546		146.00	C
ATOM	11584	CE	LYS F	89	1.075	41.298	20.484		156.99	C
ATOM	11585	NZ	LYS F	89	−0.193	41.656	21.180		156.00	N1+
ATOM	11586	H	LYS F	89	−2.667	38.200	17.840		122.93	H
ATOM	11587	HA	LYS F	89	−1.661	40.216	16.321		128.53	H
ATOM	11588	HB2	LYS F	89	−0.286	38.390	17.970		131.86	H
ATOM	11589	HB3	LYS F	89	0.475	39.318	16.930		131.86	H
ATOM	11590	HG2	LYS F	89	−0.064	41.197	18.104		139.04	H
ATOM	11591	HG3	LYS F	89	−1.062	40.384	19.040		139.04	H
ATOM	11592	HD2	LYS F	89	0.695	39.330	20.080		155.20	H
ATOM	11593	HD3	LYS F	89	1.732	39.982	19.064		155.20	H
ATOM	11594	HE2	LYS F	89	1.737	41.076	21.158		168.38	H
ATOM	11595	HE3	LYS F	89	1.366	42.069	19.972		168.38	H
ATOM	11596	HZ1	LYS F	89	−0.817	41.870	20.583		167.20	H
ATOM	11597	HZ2	LYS F	89	−0.479	40.965	21.663		167.20	H
ATOM	11598	HZ3	LYS F	89	−0.058	42.350	21.720		167.20	H
ATOM	11599	N	SER F	90	−1.243	39.015	14.259		120.20	N
ATOM	11600	CA	SER F	90	−1.063	38.297	13.002		120.82	C
ATOM	11601	C	SER F	90	0.418	38.076	12.691		121.90	C
ATOM	11602	O	SER F	90	1.195	39.028	12.641		119.40	O
ATOM	11603	CB	SER F	90	−1.719	39.065	11.852		122.35	C
ATOM	11604	OG	SER F	90	−3.108	39.241	12.070		120.82	O
ATOM	11605	H	SER F	90	−1.223	39.870	14.171		124.24	H
ATOM	11606	HA	SER F	90	−1.490	37.428	13.068		124.98	H
ATOM	11607	HB2	SER F	90	−1.300	39.937	11.779		126.83	H
ATOM	11608	HB3	SER F	90	−1.591	38.568	11.029		126.83	H
ATOM	11609	HG	SER F	90	−3.486	38.493	12.133		124.99	H
ATOM	11610	N	THR F	91	0.805	36.820	12.486		114.45	N
ATOM	11611	CA	THR F	91	2.164	36.504	12.056		122.20	C
ATOM	11612	C	THR F	91	2.125	35.449	10.960		121.21	C
ATOM	11613	O	THR F	91	1.136	34.728	10.808		120.13	O
ATOM	11614	CB	THR F	91	3.048	36.012	13.223		122.36	C
ATOM	11615	OG1	THR F	91	2.488	34.825	13.793		121.83	O
ATOM	11616	CG2	THR F	91	3.171	37.091	14.297		125.53	C
ATOM	11617	H	THR F	91	0.299	36.132	12.589		117.34	H
ATOM	11618	HA	THR F	91	2.571	37.304	11.688		126.63	H
ATOM	11619	HB	THR F	91	3.937	35.816	12.888		126.83	H
ATOM	11620	HG1	THR F	91	2.443	34.221	13.212		126.19	H
ATOM	11621	HG21	THR F	91	3.727	36.772	15.025		130.64	H
ATOM	11622	HG22	THR F	91	3.571	37.890	13.920		130.64	H
ATOM	11623	HG23	THR F	91	2.293	37.312	14.646		130.64	H
ATOM	11624	N	PHE F	92	3.210	35.371	10.198		118.86	N
ATOM	11625	CA	PHE F	92	3.250	34.542	9.005		117.69	C
ATOM	11626	C	PHE F	92	4.564	33.793	8.890		121.66	C
ATOM	11627	O	PHE F	92	5.582	34.199	9.449		117.52	O
ATOM	11628	CB	PHE F	92	3.034	35.404	7.762		116.77	C
ATOM	11629	CG	PHE F	92	1.834	36.297	7.852		117.86	C
ATOM	11630	CD1	PHE F	92	0.583	35.834	7.480		120.94	C
ATOM	11631	CD2	PHE F	92	1.955	37.598	8.316		119.25	C
ATOM	11632	CE1	PHE F	92	−0.527	36.654	7.567		120.21	C
ATOM	11633	CE2	PHE F	92	0.852	38.419	8.407		121.07	C
ATOM	11634	CZ	PHE F	92	−0.390	37.951	8.033		118.70	C
ATOM	11635	H	PHE F	92	3.942	35.793	10.354		122.63	H
ATOM	11636	HA	PHE F	92	2.533	33.890	9.047		121.23	H
ATOM	11637	HB2	PHE F	92	3.814	35.967	7.632		120.13	H
ATOM	11638	HB3	PHE F	92	2.915	34.823	6.994		120.13	H
ATOM	11639	HD1	PHE F	92	0.489	34.963	7.168		125.13	H
ATOM	11640	HD2	PHE F	92	2.790	37.919	8.571		123.10	H
ATOM	11641	HE1	PHE F	92	−1.363	36.335	7.314		124.25	H
ATOM	11642	HE2	PHE F	92	0.946	39.290	8.719		125.28	H
ATOM	11643	HZ	PHE F	92	−1.134	38.506	8.092		122.43	H
ATOM	11644	N	ASP F	93	4.528	32.693	8.151		118.85	N
ATOM	11645	CA	ASP F	93	5.714	31.893	7.904		119.59	C
ATOM	11646	C	ASP F	93	5.583	31.237	6.539		121.25	C
ATOM	11647	O	ASP F	93	4.484	30.852	6.130		115.85	O
ATOM	11648	CB	ASP F	93	5.887	30.841	9.000		123.31	C
ATOM	11649	CG	ASP F	93	7.131	29.997	8.810		131.07	C
ATOM	11650	OD1	ASP F	93	8.143	30.533	8.309		132.52	O1−
ATOM	11651	OD2	ASP F	93	7.093	28.797	9.164		133.33	O
ATOM	11652	H	ASP F	93	3.817	32.386	7.778		122.62	H
ATOM	11653	HA	ASP F	93	6.497	32.466	7.898		123.51	H
ATOM	11654	HB2	ASP F	93	5.955	31.288	9.859		127.98	H
ATOM	11655	HB3	ASP F	93	5.119	30.249	8.994		127.98	H
ATOM	11656	N	GLN F	94	6.695	31.128	5.825		116.48	N
ATOM	11657	CA	GLN F	94	6.698	30.390	4.575		121.95	C
ATOM	11658	C	GLN F	94	8.029	29.686	4.368		120.37	C
ATOM	11659	O	GLN F	94	9.078	30.195	4.754		117.80	O
ATOM	11660	CB	GLN F	94	6.378	31.314	3.394		116.26	C
ATOM	11661	CG	GLN F	94	7.372	32.427	3.149		121.74	C
ATOM	11662	CD	GLN F	94	7.010	33.272	1.933		128.61	C
ATOM	11663	OE1	GLN F	94	5.878	33.231	1.442		123.71	O
ATOM	11664	NE2	GLN F	94	7.976	34.041	1.440		134.71	N
ATOM	11665	H	GLN F	94	7.454	31.469	6.042		119.77	H
ATOM	11666	HA	GLN F	94	6.007	29.709	4.613		126.34	H
ATOM	11667	HB2	GLN F	94	6.337	30.777	2.587		119.52	H
ATOM	11668	HB3	GLN F	94	5.513	31.725	3.553		119.52	H
ATOM	11669	HG2	GLN F	94	7.393	33.009	3.925		126.09	H
ATOM	11670	HG3	GLN F	94	8.249	32.042	2.998		126.09	H
ATOM	11671	HE21	GLN F	94	7.823	34.537	0.754		141.66	H
ATOM	11672	HE22	GLN F	94	8.754	34.042	1.806		141.66	H
ATOM	11673	N	ASP F	95	7.961	28.494	3.780		119.52	N
ATOM	11674	CA	ASP F	95	9.139	27.680	3.502		119.57	C
ATOM	11675	C	ASP F	95	9.090	27.193	2.064		121.52	C
ATOM	11676	O	ASP F	95	8.010	27.017	1.496		117.71	O
ATOM	11677	CB	ASP F	95	9.219	26.471	4.443		124.75	C
ATOM	11678	CG	ASP F	95	9.408	26.861	5.898		136.23	C
ATOM	11679	OD1	ASP F	95	10.173	27.809	6.181		135.86	O
ATOM	11680	OD2	ASP F	95	8.792	26.202	6.762		136.50	O1−
ATOM	11681	H	ASP F	95	7.225	28.128	3.527		123.42	H
ATOM	11682	HA	ASP F	95	9.939	28.216	3.619		123.48	H
ATOM	11683	HB2	ASP F	95	8.395	25.964	4.375		129.70	H
ATOM	11684	HB3	ASP F	95	9.971	25.918	4.182		129.70	H
ATOM	11685	N	TYR F	96	10.266	26.978	1.488		117.67	N
ATOM	11686	CA	TYR F	96	10.397	26.363	0.173		117.08	C
ATOM	11687	C	TYR F	96	11.265	25.123	0.294		120.00	C
ATOM	11688	O	TYR F	96	12.344	25.188	0.880		120.02	O
ATOM	11689	CB	TYR F	96	11.028	27.329	−0.828		118.79	C
ATOM	11690	CG	TYR F	96	10.392	28.694	−0.885		116.85	C
ATOM	11691	CD1	TYR F	96	10.737	29.681	0.029		118.78	C
ATOM	11692	CD2	TYR F	96	9.463	29.005	−1.866		117.98	C
ATOM	11693	CE1	TYR F	96	10.164	30.932	−0.025		120.39	C
ATOM	11694	CE2	TYR F	96	8.886	30.254	−1.929		116.11	C
ATOM	11695	CZ	TYR F	96	9.239	31.214	−1.006		120.26	C
ATOM	11696	OH	TYR F	96	8.666	32.462	−1.069		122.81	O
ATOM	11697	H	TYR F	96	11.020	27.185	1.848		121.20	H
ATOM	11698	HA	TYR F	96	9.523	26.101	−0.155		120.50	H
ATOM	11699	HB2	TYR F	96	11.962	27.451	−0.593		122.55	H
ATOM	11700	HB3	TYR F	96	10.965	26.940	−1.715		122.55	H
ATOM	11701	HD1	TYR F	96	11.361	29.492	0.692		122.54	H
ATOM	11702	HD2	TYR F	96	9.223	28.358	−2.489		121.57	H
ATOM	11703	HE1	TYR F	96	10.401	31.583	0.595		124.47	H
ATOM	11704	HE2	TYR F	96	8.261	30.447	−2.590		119.33	H
ATOM	11705	HH	TYR F	96	8.124	32.497	−1.710		127.37	H
ATOM	11706	N	LEU F	97	10.806	24.001	−0.258		119.54	N
ATOM	11707	CA	LEU F	97	11.617	22.782	−0.290		121.34	C
ATOM	11708	C	LEU F	97	11.827	22.285	−1.721		121.46	C
ATOM	11709	O	LEU F	97	10.891	22.245	−2.520		115.94	O
ATOM	11710	CB	LEU F	97	10.973	21.670	0.540		121.85	C
ATOM	11711	CG	LEU F	97	10.355	22.043	1.891		124.09	C
ATOM	11712	CD1	LEU F	97	9.634	20.841	2.480		134.93	C
ATOM	11713	CD2	LEU F	97	11.413	22.551	2.856		131.03	C
ATOM	11714	H	LEU F	97	10.031	23.918	−0.621		123.45	H
ATOM	11715	HA	LEU F	97	12.488	22.973	0.091		125.61	H
ATOM	11716	HB2	LEU F	97	10.267	21.272	0.008		126.22	H
ATOM	11717	HB3	LEU F	97	11.652	21.000	0.717		126.22	H
ATOM	11718	HG	LEU F	97	9.704	22.749	1.758		128.91	H
ATOM	11719	HD11	LEU F	97	9.248	21.092	3.334		141.92	H
ATOM	11720	HD12	LEU F	97	8.934	20.563	1.869		141.92	H
ATOM	11721	HD13	LEU F	97	10.271	20.120	2.603		141.92	H
ATOM	11722	HD21	LEU F	97	10.989	22.777	3.699		137.24	H
ATOM	11723	HD22	LEU F	97	12.074	21.855	2.995		137.24	H
ATOM	11724	HD23	LEU F	97	11.835	23.338	2.476		137.24	H
ATOM	11725	N	TYR F	98	13.066	21.914	−2.030		121.23	N
ATOM	11726	CA	TYR F	98	13.397	21.259	−3.293		118.28	C
ATOM	11727	C	TYR F	98	13.879	19.850	−2.981		122.72	C
ATOM	11728	O	TYR F	98	14.924	19.675	−2.353		120.74	O
ATOM	11729	CB	TYR F	98	14.465	22.044	−4.058		118.19	C
ATOM	11730	CG	TYR F	98	14.779	21.475	−5.426		121.19	C
ATOM	11731	CD1	TYR F	98	13.950	21.729	−6.511		123.23	C
ATOM	11732	CD2	TYR F	98	15.905	20.689	−5.632		123.20	C
ATOM	11733	CE1	TYR F	98	14.233	21.213	−7.764		129.19	C
ATOM	11734	CE2	TYR F	98	16.196	20.170	−6.879		124.25	C
ATOM	11735	CZ	TYR F	98	15.357	20.434	−7.941		127.82	C
ATOM	11736	OH	TYR F	98	15.644	19.918	−9.183		133.31	O
ATOM	11737	H	TYR F	98	13.744	22.032	−1.515		125.47	H
ATOM	11738	HA	TYR F	98	12.603	21.199	−3.846		121.94	H
ATOM	11739	HB2	TYR F	98	14.157	22.955	−4.179		121.83	H
ATOM	11740	HB3	TYR F	98	15.286	22.041	−3.541		121.83	H
ATOM	11741	HD1	TYR F	98	13.192	22.254	−6.393		127.87	H
ATOM	11742	HD2	TYR F	98	16.473	20.508	−4.918		127.84	H
ATOM	11743	HE1	TYR F	98	13.668	21.391	−8.482		135.03	H
ATOM	11744	HE2	TYR F	98	16.953	19.644	−7.001		129.10	H
ATOM	11745	HH	TYR F	98	15.057	20.155	−9.736		139.98	H
ATOM	11746	N	ASN F	99	13.103	18.855	−3.405		120.11	N
ATOM	11747	CA	ASN F	99	13.368	17.458	−3.066		123.25	C
ATOM	11748	C	ASN F	99	13.517	17.267	−1.558		125.58	C
ATOM	11749	O	ASN F	99	14.394	16.536	−1.090		121.44	O
ATOM	11750	CB	ASN F	99	14.621	16.955	−3.789		122.66	C
ATOM	11751	CG	ASN F	99	14.430	16.862	−5.291		124.21	C
ATOM	11752	OD1	ASN F	99	13.320	16.636	−5.779		125.43	O
ATOM	11753	ND2	ASN F	99	15.517	17.028	−6.034		121.89	N
ATOM	11754	H	ASN F	99	12.407	18.965	−3.899		124.13	H
ATOM	11755	HA	ASN F	99	12.619	16.918	−3.360		127.90	H
ATOM	11756	HB2	ASN F	99	15.353	17.567	−3.617		127.19	H
ATOM	11757	HB3	ASN F	99	14.842	16.070	−3.459		127.19	H
ATOM	11758	HD21	ASN F	99	15.462	16.985	−6.891		126.27	H
ATOM	11759	HD22	ASN F	99	16.275	17.180	−5.658		126.27	H
ATOM	11760	N	GLY F	100	12.658	17.940	−0.799		120.75	N
ATOM	11761	CA	GLY F	100	12.618	17.775	0.642		127.43	C
ATOM	11762	C	GLY F	100	13.626	18.633	1.379		125.00	C
ATOM	11763	O	GLY F	100	13.587	18.729	2.607		123.15	O
ATOM	11764	H	GLY F	100	12.084	18.504	−1.103		124.90	H
ATOM	11765	HA2	GLY F	100	11.732	18.004	0.965		132.92	H
ATOM	11766	HA3	GLY F	100	12.792	16.847	0.862		132.92	H
ATOM	11767	N	GLU F	101	14.529	19.255	0.628		127.20	N
ATOM	11768	CA	GLU F	101	15.572	20.100	1.201		128.99	C
ATOM	11769	C	GLU F	101	15.137	21.559	1.206		126.31	C
ATOM	11770	O	GLU F	101	14.827	22.123	0.158		122.95	O
ATOM	11771	CB	GLU F	101	16.874	19.947	0.413		128.96	C
ATOM	11772	CG	GLU F	101	18.114	20.440	1.148		143.62	C
ATOM	11773	CD	GLU F	101	18.632	19.442	2.169		155.65	C
ATOM	11774	OE1	GLU F	101	18.669	18.230	1.862		148.87	O
ATOM	11775	OE2	GLU F	101	19.007	19.872	3.280		157.62	O1−
ATOM	11776	H	GLU F	101	14.560	19.203	−0.230		132.65	H
ATOM	11777	HA	GLU F	101	15.737	19.828	2.117		134.79	H
ATOM	11778	HB2	GLU F	101	17.006	19.008	0.209		134.75	H
ATOM	11779	HB3	GLU F	101	16.799	20.453	−0.411		134.75	H
ATOM	11780	HG2	GLU F	101	18.819	20.603	0.503		152.34	H
ATOM	11781	HG3	GLU F	101	17.897	21.262	1.616		152.34	H
ATOM	11782	N	GLU F	102	15.126	22.176	2.383		128.54	N
ATOM	11783	CA	GLU F	102	14.689	23.561	2.500		125.54	C
ATOM	11784	C	GLU F	102	15.733	24.512	1.927		124.67	C
ATOM	11785	O	GLU F	102	16.936	24.287	2.062		121.93	O
ATOM	11786	CB	GLU F	102	14.396	23.912	3.962		133.49	C
ATOM	11787	CG	GLU F	102	13.833	25.312	4.156		137.89	C
ATOM	11788	CD	GLU F	102	13.340	25.561	5.574		147.13	C
ATOM	11789	OE1	GLU F	102	13.153	26.742	5.939		146.84	O
ATOM	11790	OE2	GLU F	102	13.134	24.578	6.319		151.60	O1−
ATOM	11791	H	GLU F	102	15.366	21.816	3.126		134.25	H
ATOM	11792	HA	GLU F	102	13.869	23.677	1.995		130.65	H
ATOM	11793	HB2	GLU F	102	13.749	23.281	4.312		140.19	H
ATOM	11794	HB3	GLU F	102	15.221	23.852	4.469		140.19	H
ATOM	11795	HG2	GLU F	102	14.527	25.961	3.962		145.47	H
ATOM	11796	HG3	GLU F	102	13.084	25.437	3.553		145.47	H
ATOM	11797	N	TYR F	103	15.269	25.577	1.284		119.00	N
ATOM	11798	CA	TYR F	103	16.175	26.558	0.700		123.12	C
ATOM	11799	C	TYR F	103	15.507	27.925	0.622		124.60	C
ATOM	11800	O	TYR F	103	14.283	28.026	0.729		118.78	O
ATOM	11801	CB	TYR F	103	16.632	26.099	−0.686		118.11	C
ATOM	11802	CG	TYR F	103	15.564	26.151	−1.759		120.57	C
ATOM	11803	CD1	TYR F	103	14.489	25.272	−1.743		119.73	C
ATOM	11804	CD2	TYR F	103	15.647	27.066	−2.802		119.76	C
ATOM	11805	CE1	TYR F	103	13.516	25.314	−2.731		117.89	C
ATOM	11806	CE2	TYR F	103	14.681	27.117	−3.790		115.45	C
ATOM	11807	CZ	TYR F	103	13.618	26.236	−3.751		118.31	C
ATOM	11808	OH	TYR F	103	12.652	26.280	−4.734		117.87	O
ATOM	11809	H	TYR F	103	14.435	25.755	1.172		122.80	H
ATOM	11810	HA	TYR F	103	16.960	26.639	1.265		127.75	H
ATOM	11811	HB2	TYR F	103	17.364	26.667	−0.974		121.74	H
ATOM	11812	HB3	TYR F	103	16.939	25.181	−0.622		121.74	H
ATOM	11813	HD1	TYR F	103	14.417	24.650	−1.056		123.67	H
ATOM	11814	HD2	TYR F	103	16.362	27.660	−2.831		123.72	H
ATOM	11815	HE1	TYR F	103	12.798	24.722	−2.705		121.47	H
ATOM	11816	HE2	TYR F	103	14.749	27.738	−4.479		118.54	H
ATOM	11817	HH	TYR F	103	12.834	26.883	−5.290		121.44	H
ATOM	11818	N	THR F	104	16.319	28.969	0.452		120.25	N
ATOM	11819	CA	THR F	104	15.819	30.341	0.376		119.66	C
ATOM	11820	C	THR F	104	16.621	31.227	−0.581		124.00	C
ATOM	11821	O	THR F	104	16.243	32.373	−0.830		125.47	O
ATOM	11822	CB	THR F	104	15.834	31.022	1.762		123.07	C
ATOM	11823	OG1	THR F	104	17.182	31.117	2.235		127.80	O
ATOM	11824	CG2	THR F	104	14.996	30.247	2.763		127.54	C
ATOM	11825	H	THR F	104	17.174	28.907	0.378		124.30	H
ATOM	11826	HA	THR F	104	14.901	30.322	0.064		123.59	H
ATOM	11827	HB	THR F	104	15.461	31.914	1.682		127.69	H
ATOM	11828	HG1	THR F	104	17.196	31.487	2.989		133.36	H
ATOM	11829	HG21	THR F	104	15.017	30.689	3.626		133.05	H
ATOM	11830	HG22	THR F	104	14.077	30.196	2.457		133.05	H
ATOM	11831	HG23	THR F	104	15.345	29.347	2.861		133.05	H
ATOM	11832	N	VAL F	105	17.720	30.704	−1.118		121.71	N
ATOM	11833	CA	VAL F	105	18.623	31.506	−1.936		119.03	C
ATOM	11834	C	VAL F	105	18.462	31.235	−3.432		121.46	C
ATOM	11835	O	VAL F	105	18.561	30.094	−3.889		120.83	O
ATOM	11836	CB	VAL F	105	20.087	31.255	−1.536		126.65	C
ATOM	11837	CG1	VAL F	105	21.028	32.107	−2.377		128.48	C
ATOM	11838	CG2	VAL F	105	20.282	31.546	−0.051		123.67	C
ATOM	11839	H	VAL F	105	17.965	29.885	−1.023		126.06	H
ATOM	11840	HA	VAL F		105	18.430	32.445	−1.784		122.83	H
ATOM	11841	HB	VAL F	105	20.304	30.322	−1.692		131.98	H
ATOM	11842	HG11	VAL F	105	21.942	31.930	−2.105		134.18	H
ATOM	11843	HG12	VAL F	105	20.910	31.879	−3.312		134.18	H
ATOM	11844	HG13	VAL F	105	20.816	33.043	−2.236		134.18	H
ATOM	11845	HG21	VAL F	105	21.209	31.382	0.183		128.41	H
ATOM	11846	HG22	VAL F	105	20.056	32.474	0.121		128.41	H
ATOM	11847	HG23	VAL F		105	19.703	30.963	0.464		128.41	H
ATOM	11848	N	LYS F	106	18.229	32.302	−4.187		119.36	N
ATOM	11849	CA	LYS F	106	18.092	32.220	−5.634		129.10	C
ATOM	11850	C	LYS F	106	19.465	32.283	−6.295		129.24	C
ATOM	11851	O	LYS F	106	20.302	33.093	−5.904		132.55	O
ATOM	11852	CB	LYS F	106	17.203	33.358	−6.144		129.53	C
ATOM	11853	CG	LYS F	106	17.008	33.392	−7.652		135.32	C
ATOM	11854	CD	LYS F	106	16.478	34.740	−8.106		137.47	C
ATOM	11855	CE	LYS F	106	16.168	34.747	−9.600		150.78	C
ATOM	11856	NZ	LYS F	106	17.386	34.542	−10.437		152.11	N1+
ATOM	11857	H	LYS F	106	18.145	33.100	−3.877		123.23	H
ATOM	11858	HA	LYS F	106	17.676	31.377	−5.871		134.92	H
ATOM	11859	HB2	LYS F	106	16.327	33.272	−5.738		135.44	H
ATOM	11860	HB3	LYS F	106	17.602	34.203	−5.882		135.44	H
ATOM	11861	HG2	LYS F	106	17.859	33.236	−8.090		142.38	H
ATOM	11862	HG3	LYS F	106	16.367	32.710	−7.909		142.38	H
ATOM	11863	HD2	LYS F	106	15.660	34.941	−7.626		144.96	H
ATOM	11864	HD3	LYS F	106	17.145	35.422	−7.932		144.96	H
ATOM	11865	HE2	LYS F	106	15.544	34.031	−9.797		160.93	H
ATOM	11866	HE3	LYS F	106	15.779	35.603	−9.839		160.93	H
ATOM	11867	HZ1	LYS F	106	17.166	34.552	−11.300		162.53	H
ATOM	11868	HZ2	LYS F	106	17.975	35.191	−10.281		162.53	H
ATOM	11869	HZ3	LYS F	106	17.760	33.758	−10.243		162.53	H
ATOM	11870	N	THR F	107	19.691	31.424	−7.287		131.35	N
ATOM	11871	CA	THR F	107	20.912	31.469	−8.090		136.12	C
ATOM	11872	C	THR F	107	20.608	32.090	−9.449		143.02	C
ATOM	11873	O	THR F	107	19.463	32.429	−9.740		133.93	O
ATOM	11874	CB	THR F	107	21.524	30.071	−8.287		139.11	C
ATOM	11875	OG1	THR F	107	20.604	29.231	−8.994		141.98	O
ATOM	11876	CG2	THR F	107	21.855	29.442	−6.942		137.13	C
ATOM	11877	H	THR F	107	19.147	30.798	−7.517		137.62	H
ATOM	11878	HA	THR F	107	21.567	32.026	−7.642		143.34	H
ATOM	11879	HB	THR F	107	22.345	30.149	−8.797		146.93	H
ATOM	11880	HG1	THR F	107	20.936	28.468	−9.103		150.37	H
ATOM	11881	HG21	THR F	107	22.240	28.562	−7.073		144.55	H
ATOM	11882	HG22	THR F	107	22.491	29.997	−6.464		144.55	H
ATOM	11883	HG23	THR F	107	21.048	29.357	−6.409		144.55	H
ATOM	11884	N	GLN F	108	21.632	32.231	−10.284		147.01	N
ATOM	11885	CA	GLN F	108	21.497	32.983	−11.527		154.07	C
ATOM	11886	C	GLN F	108	20.864	32.173	−12.657		153.72	C
ATOM	11887	O	GLN F	108	20.083	32.708	−13.446		154.72	O
ATOM	11888	CB	GLN F	108	22.867	33.498	−11.976		167.40	C
ATOM	11889	CG	GLN F	108	23.526	34.461	−10.992		174.36	C
ATOM	11890	CD	GLN F	108	22.732	35.740	−10.791		178.47	C
ATOM	11891	OE1	GLN F	108	21.891	36.101	−11.615		179.85	O
ATOM	11892	NE2	GLN F	108	22.997	36.433	−9.688		178.07	N
ATOM	11893	H	GLN F	108	22.415	31.902	−10.154		156.42	H
ATOM	11894	HA	GLN F	108	20.930	33.753	−11.364		164.88	H
ATOM	11895	HB2	GLN F	108	23.462	32.741	−12.091		180.88	H
ATOM	11896	HB3	GLN F	108	22.763	33.965	−12.820		180.88	H
ATOM	11897	HG2	GLN F	108	23.610	34.022	−10.130		189.23	H
ATOM	11898	HG3	GLN F	108	24.403	34.703	−11.327		189.23	H
ATOM	11899	HE21	GLN F	108	22.575	37.165	−9.529		193.69	H
ATOM	11900	HE22	GLN F	108	23.591	36.149	−9.135		193.69	H
ATOM	11901	N	GLU F	109	21.200	30.890	−12.737		154.38	N
ATOM	11902	CA	GLU F	109	20.771	30.063	−13.861		155.52	C
ATOM	11903	C	GLU F	109	19.268	29.776	−13.827		149.42	C
ATOM	11904	O	GLU F	109	18.635	29.804	−12.770		141.41	O
ATOM	11905	CB	GLU F	109	21.559	28.746	−13.896		159.16	C
ATOM	11906	CG	GLU F	109	21.309	27.793	−12.727		162.14	C
ATOM	11907	CD	GLU F	109	22.090	28.152	−11.473		166.16	C
ATOM	11908	OE1	GLU F	109	22.681	29.252	−11.421		164.71	O
ATOM	11909	OE2	GLU F	109	22.112	27.325	−10.536		167.28	O1−
ATOM	11910	H	GLU F	109	21.676	30.474	−12.154		165.26	H
ATOM	11911	HA	GLU F	109	20.960	30.540	−14.685		166.62	H
ATOM	11912	HB2	GLU F	109	21.328	28.272	−14.711		170.99	H
ATOM	11913	HB3	GLU F	109	22.506	28.955	−13.902		170.99	H
ATOM	11914	HG2	GLU F	109	20.365	27.812	−12.505		174.57	H
ATOM	11915	HG3	GLU F	109	21.567	26.897	−12.992		174.57	H
ATOM	11916	N	ALA F	110	18.709	29.500	−15.002		143.62	N
ATOM	11917	CA	ALA F	110	17.279	29.251	−15.145		141.53	C
ATOM	11918	C	ALA F	110	16.936	27.807	−14.800		141.29	C
ATOM	11919	O	ALA F	110	17.257	26.886	−15.551		139.37	O
ATOM	11920	CB	ALA F	110	16.829	29.575	−16.559		142.06	C
ATOM	11921	H	ALA F	110	19.144	29.450	−15.742		152.34	H
ATOM	11922	HA	ALA F	110	16.795	29.829	−14.535		149.84	H
ATOM	11923	HB1	ALA F	110	15.877	29.403	−16.634		150.48	H
ATOM	11924	HB2	ALA F	110	17.012	30.510	−16.742		150.48	H
ATOM	11925	HB3	ALA F	110	17.317	29.014	−17.182		150.48	H
ATOM	11926	N	THR F	111	16.278	27.623	−13.659		131.19	N
ATOM	11927	CA	THR F	111	15.901	26.300	−13.185		128.12	C
ATOM	11928	C	THR F	111	14.513	26.335	−12.563		126.09	C
ATOM	11929	O	THR F	111	14.038	27.391	−12.146		123.00	O
ATOM	11930	CB	THR F	111	16.895	25.766	−12.140		131.61	C
ATOM	11931	OG1	THR F	111	16.881	26.618	−10.986		123.43	O
ATOM	11932	CG2	THR F	111	18.309	25.704	−12.718		134.93	C
ATOM	11933	H	THR F	111	16.036	28.261	−13.136		137.43	H
ATOM	11934	HA	THR F	111	15.885	25.683	−13.933		133.75	H
ATOM	11935	HB	THR F	111	16.634	24.869	−11.879		137.94	H
ATOM	11936	HG1	THR F	111	17.422	26.332	−10.411		128.12	H
ATOM	11937	HG21	THR F	111	18.925	25.366	−12.050		141.92	H
ATOM	11938	HG22	THR F	111	18.326	25.115	−13.489		141.92	H
ATOM	11939	HG23	THR F	111	18.594	26.590	−12.992		141.92	H
ATOM	11940	N	ASN F	112	13.867	25.178	−12.499		121.68	N
ATOM	11941	CA	ASN F	112	12.586	25.072	−11.820		122.81	C
ATOM	11942	C	ASN F	112	12.736	25.457	−10.350		122.60	C
ATOM	11943	O	ASN F	112	11.832	26.046	−9.758		118.34	O
ATOM	11944	CB	ASN F	112	12.023	23.655	−11.945		125.23	C
ATOM	11945	CG	ASN F	112	11.577	23.326	−13.359		130.83	C
ATOM	11946	OD1	ASN F	112	11.337	24.221	−14.171		129.96	O
ATOM	11947	ND2	ASN F	112	11.458	22.038	−13.658		131.13	N
ATOM	11948	H	ASN F	112	14.149	24.441	−12.841		126.01	H
ATOM	11949	HA	ASN F	112	11.956	25.685	−12.230		127.37	H
ATOM	11950	HB2	ASN F	112	12.709	23.019	−11.691		130.28	H
ATOM	11951	HB3	ASN F	112	11.255	23.567	−11.360		130.28	H
ATOM	11952	HD21	ASN F	112	11.209	21.801	−14.446		137.36	H
ATOM	11953	HD22	ASN F	112	11.631	21.441	−13.063		137.36	H
ATOM	11954	N	LYS F	113	13.890	25.129	−9.774		118.06	N
ATOM	11955	CA	LYS F	113	14.159	25.425	−8.374		117.23	C
ATOM	11956	C	LYS F	113	14.117	26.924	−8.124		115.57	C
ATOM	11957	O	LYS F	113	13.505	27.381	−7.160		120.36	O
ATOM	11958	CB	LYS F	113	15.518	24.858	−7.957		122.25	C
ATOM	11959	CG	LYS F	113	15.804	24.952	−6.465		119.36	C
ATOM	11960	CD	LYS F	113	17.161	24.356	−6.130		125.27	C
ATOM	11961	CE	LYS F	113	17.450	24.430	−4.645		123.84	C
ATOM	11962	NZ	LYS F	113	18.808	23.913	−4.317		130.60	N1+
ATOM	11963	H	LYS F	113	14.537	24.732	−10.178		121.67	H
ATOM	11964	HA	LYS F	113	13.477	25.009	−7.824		120.67	H
ATOM	11965	HB2	LYS F	113	15.553	23.921	−8.206		126.70	H
ATOM	11966	HB3	LYS F	113	16.215	25.346	−8.422		126.70	H
ATOM	11967	HG2	LYS F	113	15.804	25.883	−6.196		123.23	H
ATOM	11968	HG3	LYS F	113	15.125	24.459	−5.977		123.23	H
ATOM	11969	HD2	LYS F	113	17.177	23.424	−6.397		130.32	H
ATOM	11970	HD3	LYS F	113	17.852	24.851	−6.599		130.32	H
ATOM	11971	HE2	LYS F	113	17.401	25.355	−4.356		128.61	H
ATOM	11972	HE3	LYS F	113	16.798	23.895	−4.166		128.61	H
ATOM	11973	HZ1	LYS F	113	18.878	23.062	−4.568		136.72	H
ATOM	11974	HZ2	LYS F	113	19.427	24.392	−4.741		136.72	H
ATOM	11975	HZ3	LYS F	113	18.951	23.968	−3.440		136.72	H
ATOM	11976	N	ASN F	114	14.770	27.687	−8.994		115.69	N
ATOM	11977	CA	ASN F	114	14.793	29.140	−8.867		119.32	C
ATOM	11978	C	ASN F	114	13.446	29.792	−9.159		120.12	C
ATOM	11979	O	ASN F	114	13.054	30.750	−8.496		117.64	O
ATOM	11980	CB	ASN F	114	15.845	29.734	−9.800		123.98	C
ATOM	11981	CG	ASN F	114	17.251	29.576	−9.266		126.05	C
ATOM	11982	OD1	ASN F	114	17.485	29.674	−8.060		123.54	O
ATOM	11983	ND2	ASN F	114	18.198	29.334	−10.163		128.63	N
ATOM	11984	H	ASN F	114	15.208	27.387	−9.670		118.83	H
ATOM	11985	HA	ASN F	114	15.041	29.369	−7.958		123.19	H
ATOM	11986	HB2	ASN F	114	15.798	29.283	−10.658		128.78	H
ATOM	11987	HB3	ASN F	114	15.671	30.681	−9.912		128.78	H
ATOM	11988	HD21	ASN F	114	19.015	29.237	−9.910		134.35	H
ATOM	11989	HD22	ASN F	114	17.996	29.275	−10.997		134.35	H
ATOM	11990	N	MET F	115	12.749	29.282	−10.164		118.73	N
ATOM	11991	CA	MET F	115	11.481	29.867	−10.572		122.34	C
ATOM	11992	C	MET F	115	10.409	29.580	−9.524		117.47	C
ATOM	11993	O	MET F	115	9.539	30.411	−9.270		119.13	O
ATOM	11994	CB	MET F	115	11.063	29.327	−11.943		124.76	C
ATOM	11995	CG	MET F	115	12.071	29.623	−13.060		134.49	C
ATOM	11996	SD	MET F	115	11.705	28.781	−14.614		153.25	S
ATOM	11997	CE	MET F	115	10.474	29.881	−15.303		135.96	C
ATOM	11998	H	MET F	115	12.988	28.598	−10.627		122.48	H
ATOM	11999	HA	MET F	115	11.591	30.827	−10.652		126.81	H
ATOM	12000	HB2	MET F	115	10.962	28.365	−11.883		129.71	H
ATOM	12001	HB3	MET F	115	10.217	29.732	−12.193		129.71	H
ATOM	12002	HG2	MET F	115	12.074	30.578	−13.234		141.38	H
ATOM	12003	HG3	MET F	115	12.952	29.340	−12.769		141.38	H
ATOM	12004	HE1	MET F	115	10.187	29.534	−16.162		143.15	H
ATOM	12005	HE2	MET F	115	9.719	29.930	−14.696		143.15	H
ATOM	12006	HE3	MET F	115	10.866	30.762	−15.416		143.15	H
ATOM	12007	N	TRP F	116	10.477	28.397	−8.921		115.95	N
ATOM	12008	CA	TRP F	116	9.571	28.024	−7.839		116.43	C
ATOM	12009	C	TRP F	116	9.757	28.966	−6.659		117.46	C
ATOM	12010	O	TRP F	116	8.794	29.369	−6.003		113.97	O
ATOM	12011	CB	TRP F	116	9.830	26.579	−7.413		117.21	C
ATOM	12012	CG	TRP F	116	8.910	26.053	−6.352		114.30	C
ATOM	12013	CD1	TRP F	116	9.177	25.930	−5.020		116.57	C
ATOM	12014	CD2	TRP F	116	7.579	25.557	−6.541		114.31	C
ATOM	12015	NE1	TRP F	116	8.094	25.392	−4.366		115.96	N
ATOM	12016	CE2	TRP F	116	7.098	25.158	−5.277		114.58	C
ATOM	12017	CE3	TRP F	116	6.746	25.414	−7.655		114.42	C
ATOM	12018	CZ2	TRP F	116	5.824	24.620	−5.099		117.85	C
ATOM	12019	CZ3	TRP F	116	5.477	24.887	−7.475		112.40	C
ATOM	12020	CH2	TRP F	116	5.031	24.492	−6.209		114.26	C
ATOM	12021	H	TRP F	116	11.046	27.785	−9.124		119.15	H
ATOM	12022	HA	TRP F	116	8.654	28.094	−8.146		119.71	H
ATOM	12023	HB2	TRP F	116	9.735	26.007	−8.191		120.66	H
ATOM	12024	HB3	TRP F	116	10.736	26.515	−7.071		120.66	H
ATOM	12025	HD1	TRP F	116	9.977	26.174	−4.613		119.88	H
ATOM	12026	HE1	TRP F	116	8.047	25.233	−3.522		119.16	H
ATOM	12027	HE3	TRP F	116	7.037	25.670	−8.501		117.30	H
ATOM	12028	HZ2	TRP F	116	5.522	24.363	−4.257		121.42	H
ATOM	12029	HZ3	TRP F	116	4.915	24.787	−8.210		114.88	H
ATOM	12030	HH2	TRP F	116	4.174	24.144	−6.117		117.11	H
ATOM	12031	N	LEU F	117	11.014	29.315	−6.407		118.59	N
ATOM	12032	CA	LEU F	117	11.380	30.189	−5.300		117.51	C
ATOM	12033	C	LEU F	117	10.905	31.619	−5.506		116.16	C
ATOM	12034	O	LEU F	117	10.428	32.268	−4.571		115.98	O
ATOM	12035	CB	LEU F	117	12.897	30.180	−5.108		117.18	C
ATOM	12036	CG	LEU F	117	13.448	31.119	−4.034		117.88	C
ATOM	12037	CD1	LEU F	117	12.913	30.744	−2.657		121.03	C
ATOM	12038	CD2	LEU F	117	14.966	31.092	−4.048		124.18	C
ATOM	12039	H	LEU F	117	11.687	29.052	−6.874		122.30	H
ATOM	12040	HA	LEU F	117	10.973	29.853	−4.486		121.01	H
ATOM	12041	HB2	LEU F	117	13.169	29.280	−4.870		120.62	H
ATOM	12042	HB3	LEU F	117	13.311	30.430	−5.948		120.62	H
ATOM	12043	HG	LEU F	117	13.163	32.025	−4.230		121.45	H
ATOM	12044	HD11	LEU F	117	13.279	31.355	−1.999		125.23	H
ATOM	12045	HD12	LEU F	117	11.945	30.809	−2.666		125.23	H
ATOM	12046	HD13	LEU F	117	13.182	29.835	−2.450		125.23	H
ATOM	12047	HD21	LEU F	117	15.298	31.692	−3.362		129.02	H
ATOM	12048	HD22	LEU F	117	15.266	30.187	−3.871		129.02	H
ATOM	12049	HD23	LEU F	117	15.278	31.380	−4.920		129.02	H
ATOM	12050	N	THR F	118	11.042	32.121	−6.726		113.53	N
ATOM	12051	CA	THR F	118	10.730	33.519	−6.985		118.81	C
ATOM	12052	C	THR F	118	9.255	33.762	−7.325		116.55	C
ATOM	12053	O	THR F	118	8.828	34.914	−7.373		117.08	O
ATOM	12054	CB	THR F	118	11.598	34.082	−8.133		120.28	C
ATOM	12055	OG1	THR F	118	11.412	33.302	−9.320		122.13	O
ATOM	12056	CG2	THR F	118	13.070	34.063	−7.747		126.66	C
ATOM	12057	H	THR F	118	11.311	31.679	−7.414		116.23	H
ATOM	12058	HA	THR F	118	10.933	34.031	−6.187		122.57	H
ATOM	12059	HB	THR F	118	11.341	35.000	−8.309		124.34	H
ATOM	12060	HG1	THR F	118	10.606	33.323	−9.554		126.55	H
ATOM	12061	HG21	THR F	118	13.607	34.417	−8.472		131.99	H
ATOM	12062	HG22	THR F	118	13.211	34.605	−6.955		131.99	H
ATOM	12063	HG23	THR F	118	13.352	33.153	−7.561		131.99	H
ATOM	12064	N	THR F	119	8.475	32.701	−7.541		116.31	N
ATOM	12065	CA	THR F	119	7.098	32.874	−8.023		113.93	C
ATOM	12066	C	THR F	119	6.010	32.287	−7.133		115.23	C
ATOM	12067	O	THR F	119	4.835	32.608	−7.309		115.00	O
ATOM	12068	CB	THR F	119	6.908	32.252	−9.429		115.38	C
ATOM	12069	OG1	THR F	119	6.994	30.823	−9.354		115.55	O
ATOM	12070	CG2	THR F	119	7.938	32.794	−10.407		122.64	C
ATOM	12071	H	THR F	119	8.712	31.883	−7.419		119.57	H
ATOM	12072	HA	THR F	119	6.924	33.825	−8.102		116.72	H
ATOM	12073	HB	THR F	119	6.029	32.495	−9.760		118.46	H
ATOM	12074	HG1	THR F	119	7.746	30.596	−9.056		118.65	H
ATOM	12075	HG21	THR F	119	7.806	32.396	−11.281		127.16	H
ATOM	12076	HG22	THR F	119	7.850	33.757	−10.482		127.6	H
ATOM	12077	HG23	THR F	119	8.833	32.582	−10.096		127.16	H
ATOM	12078	N	SER F	120	6.372	31.435	−6.184		114.66	N
ATOM	12079	CA	SER F	120	5.353	30.736	−5.405		113.72	C
ATOM	12080	C	SER F	120	4.494	31.689	−4.583		115.42	C
ATOM	12081	O	SER F	120	3.267	31.564	−4.561		114.45	O
ATOM	12082	CB	SER F	120	6.000	29.701	−4.490		113.00	C
ATOM	12083	OG	SER F	120	6.308	28.529	−5.215		113.36	O
ATOM	12084	H	SER F	120	7.183	31.245	−5.972		117.59	H
ATOM	12085	HA	SER F	120	4.766	30.264	−6.016		116.46	H
ATOM	12086	HB2	SER F	120	6.817	30.070	−4.121		115.60	H
ATOM	12087	HB3	SER F	120	5.382	29.479	−3.776		115.60	H
ATOM	12088	HG	SER F	120	6.841	28.709	−5.839		116.03	H
ATOM	12089	N	GLU F	121	5.127	32.640	−3.906		112.33	N
ATOM	12090	CA	GLU F	121	4.374	33.607	−3.114		115.40	C
ATOM	12091	C	GLU F	121	3.490	34.461	−4.020		115.41	C
ATOM	12092	O	GLU F	121	2.297	34.645	−3.758		113.55	O
ATOM	12093	CB	GLU F	121	5.317	34.491	−2.307		117.29	C
ATOM	12094	CG	GLU F	121	4.607	35.381	−1.317		119.47	C
ATOM	12095	CD	GLU F	121	5.568	36.252	−0.541		126.69	C
ATOM	12096	OE1	GLU F	121	6.760	35.884	−0.447		127.63	O
ATOM	12097	OE2	GLU F	121	5.132	37.303	−0.028		131.22	O1−
ATOM	12098	H	GLU F	121	5.980	32.748	−3.888		114.80	H
ATOM	12099	HA	GLU F	121	3.801	33.131	−2.493		118.48	H
ATOM	12100	HB2	GLU F	121	5.931	33.926	−1.813		120.74	H
ATOM	12101	HB3	GLU F	121	5.811	35.061	−2.918		120.74	H
ATOM	12102	HG2	GLU F	121	3.992	35.960	−1.794		123.37	H
ATOM	12103	HG3	GLU F	121	4.122	34.828	−0.684		123.37	H
ATOM	12104	N	PHE F	122	4.095	34.977	−5.083		113.83	N
ATOM	12105	CA	PHE F	122	3.375	35.708	−6.123		114.10	C
ATOM	12106	C	PHE F	122	2.122	34.964	−6.586		115.86	C
ATOM	12107	O	PHE F	122	1.038	35.545	−6.674		114.66	O
ATOM	12108	CB	PHE F	122	4.314	35.954	−7.308		115.83	C
ATOM	12109	CG	PHE F	122	3.651	36.569	−8.505		117.67	C
ATOM	12110	CD1	PHE F	122	3.586	37.944	−8.644		116.84	C
ATOM	12111	CD2	PHE F	122	3.124	35.770	−9.510		115.73	C
ATOM	12112	CE1	PHE F	122	2.991	38.512	−9.751		119.00	C
ATOM	12113	CE2	PHE F	122	2.525	36.331	−10.617		121.26	C
ATOM	12114	CZ	PHE F	122	2.461	37.707	−10.740		121.83	C
ATOM	12115	H	PHE F	122	4.940	34.915	−5.230		116.59	H
ATOM	12116	HA	PHE F	122	3.101	36.570	−5.772		116.92	H
ATOM	12117	HB2	PHE F	122	5.023	36.552	−7.024		119.00	H
ATOM	12118	HB3	PHE F	122	4.694	35.105	−7.585		119.00	H
ATOM	12119	HD1	PHE F	122	3.942	38.490	−7.982		120.21	H
ATOM	12120	HD2	PHE F	122	3.166	34.845	−9.430		118.87	H
ATOM	12121	HE1	PHE F	122	2.946	39.438	−9.831		122.80	H
ATOM	12122	HE2	PHE F	122	2.170	35.786	−11.281		125.51	H
ATOM	12123	HZ	PHE F	122	2.057	38.089	−11.485		126.20	H
ATOM	12124	N	ARG F	123	2.271	33.671	−6.857		114.87	N
ATOM	12125	CA	ARG F	123	1.185	32.875	−7.423		115.14	C
ATOM	12126	C	ARG F	123	0.102	32.529	−6.394		116.12	C
ATOM	12127	O	ARG F	123	−1.047	32.276	−6.759		115.25	O
ATOM	12128	CB	ARG F	123	1.752	31.598	−8.055		117.25	C
ATOM	12129	CG	ARG F	123	2.417	31.851	−9.407		115.66	C
ATOM	12130	CD	ARG F	123	2.949	30.582	−10.069		116.20	C
ATOM	12131	NE	ARG F	123	4.170	30.101	−9.428		117.22	N
ATOM	12132	CZ	ARG F	123	4.237	29.081	−8.574		113.04	C
ATOM	12133	NH1	ARG F	123	3.150	28.391	−8.242		111.59	N1+
ATOM	12134	NH2	ARG F	123	5.408	28.743	−8.054		113.48	N
ATOM	12135	H	ARG F	123	2.996	33.228	−6.721		117.85	H
ATOM	12136	HA	ARG F	123	0.763	33.388	−8.129		118.17	H
ATOM	12137	HB2	ARG F	123	2.418	31.220	−7.460		120.70	H
ATOM	12138	HB3	ARG F	123	1.030	30.965	−8.191		120.70	H
ATOM	12139	HG2	ARG F	123	1.767	32.250	−10.006		118.79	H
ATOM	12140	HG3	ARG F	123	3.164	32.456	−9.280		118.79	H
ATOM	12141	HD2	ARG F	123	2.278	29.884	−10.005		119.44	H
ATOM	12142	HD3	ARG F	123	3.149	30.769	−11.000		119.44	H
ATOM	12143	HE	ARG F	123	4.904	30.508	−9.617		120.67	H
ATOM	12144	HH11	ARG F	123	2.387	28.605	−8.575		113.91	H
ATOM	12145	HH12	ARG F	123	3.210	27.734	−7.691		113.91	H
ATOM	12146	HH21	ARG F	123	6.116	29.182	−8.266		116.17	H
ATOM	12147	HH22	ARG F	123	5.460	28.083	−7.505		116.17	H
ATOM	12148	N	LEU F	124	0.455	32.535	−5.113		115.08	N
ATOM	12149	CA	LEU F	124	−0.532	32.315	−4.062		116.64	C
ATOM	12150	C	LEU F	124	−1.329	33.584	−3.789		117.66	C
ATOM	12151	O	LEU F	124	−2.555	33.542	−3.651		114.64	O
ATOM	12152	CB	LEU F	124	0.137	31.848	−2.766		112.40	C
ATOM	12153	CG	LEU F	124	−0.767	31.818	−1.525		115.66	C
ATOM	12154	CD1	LEU F	124	−1.960	30.901	−1.736		118.94	C
ATOM	12155	CD2	LEU F	124	0.001	31.410	−0.273		112.65	C
ATOM	12156	H	LEU F	124	1.256	32.662	−4.827		118.10	H
ATOM	12157	HA	LEU F	124	−1.151	31.626	−4.347		119.97	H
ATOM	12158	HB2	LEU F	124	0.473	30.948	−2.903		114.88	H
ATOM	12159	HB3	LEU F	124	0.877	32.443	−2.572		114.88	H
ATOM	12160	HG	LEU F	124	−1.112	32.712	−1.376		118.80	H
ATOM	12161	HD11	LEU F	124	−2.507	30.907	−0.935		122.72	H
ATOM	12162	HD12	LEU F	124	−2.475	31.223	−2.492		122.72	H
ATOM	12163	HD13	LEU F	124	−1.639	30.003	−1.912		122.72	H
ATOM	12164	HD21	LEU F	124	−0.607	31.405	0.482		115.18	H
ATOM	12165	HD22	LEU F	124	0.373	30.524	−0.406		115.18	H
ATOM	12166	HD23	LEU F	124	0.715	32.049	−0.120		115.18	H
ATOM	12167	N	LYS F	125	−0.628	34.711	−3.714		116.52	N
ATOM	12168	CA	LYS F	125	−1.208	35.923	−3.146		113.85	C
ATOM	12169	C	LYS F	125	−1.934	36.817	−4.144		118.09	C
ATOM	12170	O	LYS F	125	−2.316	37.935	−3.802		117.06	O
ATOM	12171	CB	LYS F	125	−0.117	36.732	−2.443		116.06	C
ATOM	12172	CG	LYS F	125	0.491	36.018	−1.252		120.08	C
ATOM	12173	CD	LYS F	125	1.351	36.960	−0.420		122.60	C
ATOM	12174	CE	LYS F	125	1.664	36.362	0.940		123.37	C
ATOM	12175	NZ	LYS F	125	2.510	37.267	1.764		123.92	N1+
ATOM	12176	H	LYS F	125	0.183	34.801	−3.985		119.83	H
ATOM	12177	HA	LYS F	125	−1.854	35.662	−2.471		116.62	H
ATOM	12178	HB2	LYS F	125	0.595	36.915	−3.076		119.28	H
ATOM	12179	HB3	LYS F	125	−0.499	37.566	−2.127		119.28	H
ATOM	12180	HG2	LYS F	125	−0.219	35.674	−0.688		124.10	H
ATOM	12181	HG3	LYS F	125	1.052	35.291	−1.567		124.10	H
ATOM	12182	HD2	LYS F	125	2.188	37.123	−0.881		127.13	H
ATOM	12183	HD3	LYS F	125	0.874	37.794	−0.283		127.13	H
ATOM	12184	HE2	LYS F	125	0.834	36.205	1.417		128.04	H
ATOM	12185	HE3	LYS F	125	2.142	35.527	0.818		128.04	H
ATOM	12186	HZ1	LYS F	125	3.282	37.423	1.348		128.71	H
ATOM	12187	HZ2	LYS F	125	2.090	38.041	1.894		128.71	H
ATOM	12188	HZ3	LYS F	125	2.678	36.891	2.553		128.71	H
ATOM	12189	N	LYS F	126	−2.143	36.328	−5.363		114.39	N
ATOM	12190	CA	LYS F	126	−2.855	37.102	−6.371		115.04	C
ATOM	12191	C	LYS F	126	−4.200	37.597	−5.829		115.14	C
ATOM	12192	O	LYS F	126	−4.500	38.788	−5.906		113.71	O
ATOM	12193	CB	LYS F	126	−3.057	36.270	−7.637		115.31	C
ATOM	12194	CG	LYS F	126	−3.569	37.060	−8.822		114.58	C
ATOM	12195	CD	LYS F	126	−3.293	36.319	−10.120		118.23	C
ATOM	12196	CE	LYS F	126	−3.981	36.970	−11.302		124.64	C
ATOM	12197	NZ	LYS F	126	−3.627	36.281	−12.575		124.00	N1+
ATOM	12198	H	LYS F	126	−1.883	35.553	−5.630		117.27	H
ATOM	12199	HA	LYS F	126	−2.323	37.879	−6.605		118.05	H
ATOM	12200	HB2	LYS F	126	−2.207	35.876	−7.889		118.37	H
ATOM	12201	HB3	LYS F	126	−3.700	35.569	−7.449		118.37	H
ATOM	12202	HG2	LYS F	126	−4.528	37.183	−8.738		117.49	H
ATOM	12203	HG3	LYS F	126	−3.119	37.918	−8.857		117.49	H
ATOM	12204	HD2	LYS F	126	−2.338	36.318	−10.289		121.87	H
ATOM	12205	HD3	LYS F	126	−3.620	35.409	−10.043		121.87	H
ATOM	12206	HE2	LYS F	126	−4.943	36.917	−11.183		129.56	H
ATOM	12207	HE3	LYS F	126	−3.700	37.896	−11.367		129.56	H
ATOM	12208	HZ1	LYS F	126	−4.039	36.675	−13.258		128.80	H
ATOM	12209	HZ2	LYS F	126	−2.748	36.318	−12.706		128.80	H
ATOM	12210	HZ3	LYS F	126	−3.878	35.427	−12.538		128.80	H
ATOM	12211	N	TRP F	127	−4.983	36.690	−5.245		115.14	N
ATOM	12212	CA	TRP F	127	−6.284	37.040	−4.663		115.40	C
ATOM	12213	C	TRP F	127	−6.357	36.731	−3.163		115.55	C
ATOM	12214	O	TRP F	127	−7.408	36.886	−2.532		113.20	O
ATOM	12215	CB	TRP F	127	−7.397	36.293	−5.400		111.59	C
ATOM	12216	CG	TRP F	127	−7.543	36.706	−6.833		115.11	C
ATOM	12217	CD1	TRP F	127	−7.053	36.059	−7.931		117.05	C
ATOM	12218	CD2	TRP F	127	−8.229	37.863	−7.323		115.18	C
ATOM	12219	NE1	TRP F	127	−7.390	36.744	−9.075		117.58	N
ATOM	12220	CE2	TRP F	127	−8.114	37.854	−8.729		118.89	C
ATOM	12221	CE3	TRP F	127	−8.930	38.906	−6.710		119.66	C
ATOM	12222	CZ2	TRP F	127	−8.675	38.847	−9.531		119.66	C
ATOM	12223	CZ3	TRP F	127	−9.486	39.891	−7.507		117.24	C
ATOM	12224	CH2	TRP F	127	−9.353	39.854	−8.904		123.08	C
ATOM	12225	H	TRP F	127	−4.783	35.856	−5.172		118.17	H
ATOM	12226	HA	TRP F	127	−6.434	37.991	−4.779		118.48	H
ATOM	12227	HB2	TRP F	127	−7.202	35.343	−5.382		113.91	H
ATOM	12228	HB3	TRP F	127	−8.240	36.466	−4.953		113.91	H
ATOM	12229	HD1	TRP F	127	−6.560	35.270	−7.908		120.46	H
ATOM	12230	HE1	TRP F	127	−7.183	36.511	−9.877		121.10	H
ATOM	12231	HE3	TRP F	127	−9.022	38.937	−5.785		123.59	H
ATOM	12232	HZ2	TRP F	127	−8.589	38.826	−10.457		123.59	H
ATOM	12233	HZ3	TRP F	127	−9.954	40.589	−7.111		120.69	H
ATOM	12234	HH2	TRP F	127	−9.737	40.530	−9.415		127.70	H
ATOM	12235	N	PHE F	128	−5.230	36.311	−2.599		113.38	N
ATOM	12236	CA	PHE F	128	−5.188	35.772	−1.243		117.23	C
ATOM	12237	C	PHE F	128	−3.938	36.245	−0.498		116.62	C
ATOM	12238	O	PHE F	128	−2.925	35.552	−0.476		114.93	O
ATOM	12239	CB	PHE F	128	−5.234	34.241	−1.310		112.61	C
ATOM	12240	CG	PHE F	128	−5.412	33.567	0.020		115.61	C
ATOM	12241	CD1	PHE F	128	−6.504	33.855	0.818		117.23	C
ATOM	12242	CD2	PHE F	128	−4.503	32.619	0.454		113.57	C
ATOM	12243	CE1	PHE F	128	−6.674	33.226	2.031		114.89	C
ATOM	12244	CE2	PHE F	128	−4.668	31.985	1.669		116.18	C
ATOM	12245	CZ	PHE F	128	−5.756	32.288	2.459		114.81	C
ATOM	12246	H	PHE F	128	−4.463	36.329	−2.987		116.05	H
ATOM	12247	HA	PHE F	128	−5.967	36.079	−0.753		120.67	H
ATOM	12248	HB2	PHE F	128	−5.976	33.977	−1.876		115.13	H
ATOM	12249	HB3	PHE F	128	−4.402	33.922	−1.693		115.13	H
ATOM	12250	HD1	PHE F	128	−7.126	34.486	0.536		120.67	H
ATOM	12251	HD2	PHE F	128	−3.767	32.412	−0.075		116.29	H
ATOM	12252	HE1	PHE F	128	−7.409	33.432	2.563		117.87	H
ATOM	12253	HE2	PHE F	128	−4.047	31.355	1.954		119.41	H
ATOM	12254	HZ	PHE F	128	−5.870	31.864	3.278		117.78	H
ATOM	12255	N	ASP F	129	−4.011	37.426	0.108		116.80	N
ATOM	12256	CA	ASP F	129	−2.863	37.972	0.828		117.78	C
ATOM	12257	C	ASP F	129	−2.895	37.537	2.290		119.18	C
ATOM	12258	O	ASP F	129	−3.800	36.814	2.714		116.91	O
ATOM	12259	CB	ASP F	129	−2.819	39.504	0.714		118.37	C
ATOM	12260	CG	ASP F	129	−4.066	40.185	1.263		116.63	C
ATOM	12261	OD1	ASP F	129	−4.707	39.642	2.181		116.14	O
ATOM	12262	OD2	ASP F	129	−4.394	41.289	0.779		116.62	O1−
ATOM	12263	H	ASP F	129	−4.708	37.928	0.119		120.16	H
ATOM	12264	HA	ASP F	129	−2.050	37.621	0.432		121.34	H
ATOM	12265	HB2	ASP F	129	−2.055	39.834	1.212		122.04	H
ATOM	12266	HB3	ASP F	129	−2.734	39.747	−0.221		122.04	H
ATOM	12267	N	GLY F	130	−1.900	37.976	3.052		115.15	N
ATOM	12268	CA	GLY F	130	−1.783	37.608	4.450		117.82	C
ATOM	12269	C	GLY F	130	−2.997	37.984	5.277		116.60	C
ATOM	12270	O	GLY F	130	−3.425	37.224	6.147		114.67	O
ATOM	12271	H	GLY F	130	−1.273	38.496	2.775		118.18	H
ATOM	12272	HA2	GLY F	130	−1.654	36.649	4.518		121.38	H
ATOM	12273	HA3	GLY F	130	−1.007	38.048	4.832		121.38	H
ATOM	12274	N	GLU F	131	−3.560	39.156	5.010		113.72	N
ATOM	12275	CA	GLU F	131	−4.732	39.598	5.751		118.76	C
ATOM	12276	C	GLU F	131	−5.928	38.710	5.433		116.47	C
ATOM	12277	O	GLU F	131	−6.715	38.380	6.322		113.63	O
ATOM	12278	CB	GLU F	131	−5.052	41.056	5.440		119.73	C
ATOM	12279	CG	GLU F	131	−6.078	41.653	6.382		126.43	C
ATOM	12280	CD	GLU F	131	−6.202	43.154	6.229		127.13	C
ATOM	12281	OE1	GLU F	131	−5.568	43.715	5.309		119.31	O
ATOM	12282	OE2	GLU F	131	−6.931	43.773	7.034		131.50	O1−
ATOM	12283	H	GLU F	131	−3.285	39.709	4.412		116.47	H
ATOM	12284	HA	GLU F	131	−4.550	39.527	6.702		122.52	H
ATOM	12285	HB2	GLU F	131	−4.239	41.579	5.514		123.68	H
ATOM	12286	HB3	GLU F	131	−5.404	41.115	4.538		123.68	H
ATOM	12287	HG2	GLU F	131	−6.945	41.260	6.196		131.71	H
ATOM	12288	HG3	GLU F	131	−5.816	41.465	7.296		131.71	H
ATOM	12289	N	ASP F	132	−6.067	38.318	4.169		115.33	N
ATOM	12290	CA	ASP F	132	−7.115	37.374	3.801		113.35	C
ATOM	12291	C	ASP F	132	−6.949	36.086	4.596		114.58	C
ATOM	12292	O	ASP F	132	−7.918	35.557	5.137		115.18	O
ATOM	12293	CB	ASP F	132	−7.094	37.063	2.305		115.90	C
ATOM	12294	CG	ASP F	132	−7.322	38.286	1.444		117.33	C
ATOM	12295	OD1	ASP F	132	−8.013	39.232	1.887		116.63	O
ATOM	12296	OD2	ASP F	132	−6.809	38.292	0.308		118.06	O1−
ATOM	12297	H	ASP F	132	−5.575	38.581	3.515		118.40	H
ATOM	12298	HA	ASP F	132	−7.980	37.756	4.018		116.02	H
ATOM	12299	HB2	ASP F	132	−6.229	36.690	2.073		119.08	H
ATOM	12300	HB3	ASP F	132	−7.794	36.422	2.107		119.08	H
ATOM	12301	N	CYS F	133	−5.716	35.591	4.680		114.32	N
ATOM	12302	CA	CYS F	133	−5.449	34.328	5.364		114.59	C
ATOM	12303	C	CYS F	133	−5.892	34.382	6.825		115.41	C
ATOM	12304	O	CYS F	133	−6.499	33.441	7.328		114.68	O
ATOM	12305	CB	CYS F	133	−3.964	33.968	5.286		118.53	C
ATOM	12306	SG	CYS F	133	−3.547	32.418	6.119		124.44	S
ATOM	12307	H	CYS F	133	−5.017	35.968	4.350		117.18	H
ATOM	12308	HA	CYS F	133	−5.951	33.622	4.927		117.51	H
ATOM	12309	HB2	CYS F	133	−3.712	33.881	4.353		122.24	H
ATOM	12310	HB3	CYS F	133	−3.448	34.677	5.702		122.24	H
ATOM	12311	N	ILE F	134	−5.593	35.489	7.496		114.80	N
ATOM	12312	CA	ILE F	134	−5.980	35.661	8.890		112.54	C
ATOM	12313	C	ILE F	134	−7.507	35.701	9.031		114.20	C
ATOM	12314	O	ILE F	134	−8.068	35.120	9.957		114.69	O
ATOM	12315	CB	ILE F	134	−5.370	36.952	9.483		114.54	C
ATOM	12316	CG1	ILE F	134	−3.842	36.854	9.542		115.52	C
ATOM	12317	CG2	ILE F	134	−5.935	37.240	10.873		118.23	C
ATOM	12318	CD1	ILE F	134	−3.302	35.789	10.488		120.56	C
ATOM	12319	H	ILE F	134	−5.165	36.157	7.165		117.76	H
ATOM	12320	HA	ILE F	134	−5.650	34.908	9.406		115.05	H
ATOM	12321	HB	ILE F	134	−5.604	37.692	8.902		117.45	H
ATOM	12322	HG12	ILE F	134	−3.512	36.651	8.653		118.62	H
ATOM	12323	HG13	ILE F	134	−3.489	37.710	9.832		118.62	H
ATOM	12324	HG21	ILE F	134	−5.533	38.054	11.214		121.87	H
ATOM	12325	HG22	ILE F	134	−6.896	37.348	10.806		121.87	H
ATOM	12326	HG23	ILE F	134	−5.725	36.496	11.459		121.87	H
ATOM	12327	HD11	ILE F	134	−2.333	35.802	10.457		124.67	H
ATOM	12328	HD12	ILE F	134	−3.608	35.983	11.388		124.67	H
ATOM	12329	HD13	ILE F	134	−3.631	34.921	10.206		124.67	H
ATOM	12330	N	MET F	135	−8.184	36.386	8.117		112.68	N
ATOM	12331	CA	MET F	135	−9.635	36.491	8.203		114.96	C
ATOM	12332	C	MET F	135	−10.291	35.143	7.899		117.64	C
ATOM	12333	O	MET F	135	−11.291	34.786	8.528		118.23	O
ATOM	12334	CB	MET F	135	−10.156	37.577	7.261		115.55	C
ATOM	12335	CG	MET F	135	−9.677	38.983	7.625		118.93	C
ATOM	12336	SD	MET F	135	−10.279	39.567	9.225		125.83	S
ATOM	12337	CE	MET F	135	−11.971	39.939	8.804		123.03	C
ATOM	12338	H	MET F	135	−7.833	36.795	7.446		115.22	H
ATOM	12339	HA	MET F	135	−9.872	36.751	9.107		117.96	H
ATOM	12340	HB2	MET F	135	−9.852	37.384	6.360		118.66	H
ATOM	12341	HB3	MET F	135	−11.126	37.577	7.288		118.66	H
ATOM	12342	HG2	MET F	135	−8.707	38.985	7.655		122.72	H
ATOM	12343	HG3	MET F	135	−9.986	39.605	6.947		122.72	H
ATOM	12344	HE1	MET F	135	−12.427	40.272	9.593		127.63	H
ATOM	12345	HE2	MET F	135	−11.982	40.613	8.107		127.63	H
ATOM	12346	HE3	MET F	135	−12.403	39.129	8.490		127.63	H
ATOM	12347	N	HIS F	136	−9.727	34.394	6.950		117.74	N
ATOM	12348	CA	HIS F		136	−10.191	33.034	6.677		114.38	C
ATOM	12349	C	HIS F	136	−10.007	32.155	7.908		115.88	C
ATOM	12350	O	HIS F		136	−10.899	31.400	8.284		115.42	O
ATOM	12351	CB	HIS F	136	−9.443	32.412	5.489		116.15	C
ATOM	12352	CG	HIS F		136	−9.875	32.932	4.152		115.03	C
ATOM	12353	ND1	HIS F	136	−9.959	32.127	3.035		115.21	N
ATOM	12354	CD2	HIS F		136	−10.236	34.172	3.748		113.64	C
ATOM	12355	CE1	HIS F		136	−10.355	32.850	2.003		115.34	C
ATOM	12356	NE2	HIS F	136	−10.530	34.094	2.408		115.92	N
ATOM	12357	H	HIS F		136	−9.074	34.650	6.451		121.29	H
ATOM	12358	HA	HIS F		136	−11.136	33.058	6.461		117.26	H
ATOM	12359	HB2	HIS F	136	−8.495	32.598	5.586		119.38	H
ATOM	12360	HB3	HIS F	136	−9.591	31.453	5.495		119.38	H
ATOM	12361	HD1	HIS F		136	−9.780	31.286	3.013		118.25	H
ATOM	12362	HD2	HIS F		136	−10.277	34.935	4.279		116.36	H
ATOM	12363	HE1	HIS F	136	−10.489	32.535	1.138		118.41	H
ATOM	12364	HE2	HIS F		136	−10.788	34.749	1.914		119.10	H
ATOM	12365	N	LEU F		137	−8.833	32.255	8.523		114.21	N
ATOM	12366	CA	LEU F	137	−8.515	31.483	9.717		116.46	C
ATOM	12367	C	LEU F	137	−9.530	31.739	10.832		116.07	C
ATOM	12368	O	LEU F	137	−10.045	30.804	11.433		116.54	O
ATOM	12369	CB	LEU F	137	−7.101	31.819	10.196		116.82	C
ATOM	12370	CG	LEU F	137	−6.696	31.348	11.597		117.25	C
ATOM	12371	CD1	LEU F	137	−6.909	29.855	11.775		121.45	C
ATOM	12372	CD2	LEU F	137	−5.239	31.707	11.858		116.99	C
ATOM	12373	H	LEU F	137	−8.195	32.769	8.263		117.06	H
ATOM	12374	HA	LEU F	137	−8.542	30.538	9.499		119.75	H
ATOM	12375	HB2	LEU F	137	−6.472	31.425	9.572		120.18	H
ATOM	12376	HB3	LEU F	137	−7.000	32.784	10.182		120.18	H
ATOM	12377	HG	LEU F	137	−7.240	31.808	12.254		120.69	H
ATOM	12378	HD11	LEU F	137	−6.640	29.603	12.672		125.74	H
ATOM	12379	HD12	LEU F	137	−7.848	29.653	11.641		125.74	H
ATOM	12380	HD13	LEU F	137	−6.372	29.380	11.122		125.74	H
ATOM	12381	HD21	LEU F	137	−4.994	31.404	12.747		120.39	H
ATOM	12382	HD22	LEU F	137	−4.682	31.271	11.195		120.39	H
ATOM	12383	HD23	LEU F	137	−5.136	32.670	11.797		120.39	H
ATOM	12384	N	ARG F	138	−9.817	33.006	11.100		115.78	N
ATOM	12385	CA	ARG F	138	−10.767	33.360	12.147		121.48	C
ATOM	12386	C	ARG F	138	−12.162	32.844	11.802		120.46	C
ATOM	12387	O	ARG F	138	−12.903	32.389	12.676		117.61	O
ATOM	12388	CB	ARG F	138	−10.791	34.875	12.353		120.11	C
ATOM	12389	CG	ARG F	138	−9.496	35.437	12.926		122.32	C
ATOM	12390	CD	ARG F	138	−9.536	36.954	13.003		122.66	C
ATOM	12391	NE	ARG F	138	−10.564	37.424	13.925		125.37	N
ATOM	12392	CZ	ARG F	138	−10.969	38.686	14.016		133.49	C
ATOM	12393	NH1	ARG F	138	−10.435	39.618	13.241		130.85	N1+
ATOM	12394	NH2	ARG F	138	−11.917	39.018	14.882		135.00	N
ATOM	12395	H	ARG F	138	−9.477	33.681	10.690		118.94	H
ATOM	12396	HA	ARG F	138	−10.490	32.946	12.979		125.77	H
ATOM	12397	HB2	ARG F	138	−10.948	35.305	11.498		124.13	H
ATOM	12398	HB3	ARG F	138	−11.507	35.096	12.969		124.13	H
ATOM	12399	HG2	ARG F	138	−9.364	35.090	13.822		126.78	H
ATOM	12400	HG3	ARG F	138	−8.755	35.181	12.354		126.78	H
ATOM	12401	HD2	ARG F	138	−8.678	37.281	13.315		127.20	H
ATOM	12402	HD3	ARG F	138	−9.731	37.313	12.123		127.20	H
ATOM	12403	HE	ARG F	138	−10.932	36.845	14.443		130.44	H
ATOM	12404	HH11	ARG F	138	−9.821	39.407	12.676		137.02	H
ATOM	12405	HH12	ARG F	138	−10.700	40.433	13.303		137.02	H
ATOM	12406	HH21	ARG F	138	−12.267	38.417	15.388		142.00	H
ATOM	12407	HH22	ARG F	138	−12.178	39.836	14.942		142.00	H
ATOM	12408	N	SER F	139	−12.505	32.898	10.520		117.64	N
ATOM	12409	CA	SER F	139	−13.798	32.413	10.056		119.10	C
ATOM	12410	C	SER F	139	−13.890	30.893	10.165		120.53	C
ATOM	12411	O	SER F	139	−14.945	30.348	10.492		120.71	O
ATOM	12412	CB	SER F	139	−14.042	32.855	8.613		121.03	C
ATOM	12413	OG	SER F	139	−14.120	34.266	8.526		116.92	O
ATOM	12414	H	SER F	139	−12.003	33.212	9.896		121.17	H
ATOM	12415	HA	SER F	139	−14.496	32.797	10.609		122.92	H
ATOM	12416	HB2	SER F	139	−13.308	32.545	8.059		125.24	H
ATOM	12417	HB3	SER F	139	−14.877	32.473	8.302		125.24	H
ATOM	12418	HG	SER F	139	−13.402	34.611	8.793		120.30	H
ATOM	12419	N	LEU F	140	−12.783	30.210	9.897		117.28	N
ATOM	12420	CA	LEU F	140	−12.766	28.753	9.949		120.30	C
ATOM	12421	C	LEU F	140	−12.769	28.260	11.394		121.22	C
ATOM	12422	O	LEU F	140	−13.346	27.216	11.695		123.85	O
ATOM	12423	CB	LEU F	140	−11.554	28.201	9.195		121.20	C
ATOM	12424	CG	LEU F	140	−11.611	28.339	7.669		120.22	C
ATOM	12425	CD1	LEU F	140	−10.258	28.037	7.052		119.97	C
ATOM	12426	CD2	LEU F	140	−12.680	27.431	7.075		121.22	C
ATOM	12427	H	LEU F	140	−12.030	30.565	9.682		120.74	H
ATOM	12428	HA	LEU F	140	−13.566	28.415	9.517		124.37	H
ATOM	12429	HB2	LEU F	140	−10.762	28.671	9.500		125.44	H
ATOM	12430	HB3	LEU F	140	−11.469	27.257	9.399		125.44	H
ATOM	12431	HG	LEU F	140	−11.841	29.254	7.446		124.27	H
ATOM	12432	HD11	LEU F	140	−10.323	28.132	6.088		123.96	H
ATOM	12433	HD12	LEU F	140	−9.605	28.662	7.402		123.96	H
ATOM	12434	HD13	LEU F	140	−10.003	27.129	7.279		123.96	H
ATOM	12435	HD21	LEU F	140	−12.689	27.542	6.112		125.46	H
ATOM	12436	HD22	LEU F	140	−12.473	26.510	7.300		125.46	H
ATOM	12437	HD23	LEU F	140	−13.543	27.676	7.445		125.46	H
ATOM	12438	N	VAL F	141	−12.132	29.008	12.288		119.00	N
ATOM	12439	CA	VAL F	141	−12.164	28.668	13.704		123.28	C
ATOM	12440	C	VAL F	141	−13.590	28.802	14.237		125.21	C
ATOM	12441	O	VAL F	141	−14.020	28.017	15.081		124.34	O
ATOM	12442	CB	VAL F	141	−11.210	29.556	14.528		119.95	C
ATOM	12443	CG1	VAL F	141	−11.452	29.377	16.024		126.02	C
ATOM	12444	CG2	VAL F	141	−9.758	29.225	14.198		124.20	C
ATOM	12445	H	VAL F	141	−11.678	29.714	12.101		122.80	H
ATOM	12446	HA	VAL F	141	−11.886	27.745	13.814		127.94	H
ATOM	12447	HB	VAL F	141	−11.367	30.487	14.305		123.94	H
ATOM	12448	HG11	VAL F	141	−10.838	29.947	16.514		131.23	H
ATOM	12449	HG12	VAL F	141	−12.368	29.624	16.227		131.23	H
ATOM	12450	HG13	VAL F	141	−11.300	28.448	16.259		131.23	H
ATOM	12451	HG21	VAL F	141	−9.177	29.794	14.727		129.04	H
ATOM	12452	HG22	VAL F	141	−9.591	28.293	14.410		129.04	H
ATOM	12453	HG23	VAL F	141	−9.605	29.382	13.253		129.04	H
ATOM	12454	N	ARG F	142	−14.315	29.802	13.745		121.37	N
ATOM	12455	CA	ARG F	142	−15.718	29.978	14.107		123.25	C
ATOM	12456	C	ARG F	142	−16.534	28.742	13.722		130.62	C
ATOM	12457	O	ARG F	142	−17.319	28.235	14.525		127.61	O
ATOM	12458	CB	ARG F	142	−16.286	31.230	13.436		128.79	C
ATOM	12459	CG	ARG F	142	−17.776	31.456	13.656		134.59	C
ATOM	12460	CD	ARG F	142	−18.109	31.669	15.122		136.74	C
ATOM	12461	NE	ARG F	142	−19.526	31.963	15.311		143.29	N
ATOM	12462	CZ	ARG F	142	−20.073	33.164	15.149		147.11	C
ATOM	12463	NH1	ARG F	142	−19.325	34.201	14.794		140.67	N1+
ATOM	12464	NH2	ARG F	142	−21.373	33.330	15.342		153.09	N
ATOM	12465	H	ARG F	142	−14.017	30.395	13.197		125.65	H
ATOM	12466	HA	ARG F	142	−15.785	30.095	15.068		127.90	H
ATOM	12467	HB2	ARG F	142	−15.818	32.006	13.782		134.55	H
ATOM	12468	HB3	ARG F	142	−16.138	31.161	12.479		134.55	H
ATOM	12469	HG2	ARG F	142	−18.054	32.244	13.164		141.50	H
ATOM	12470	HG3	ARG F	142	−18.265	30.678	13.345		141.50	H
ATOM	12471	HD2	ARG F	142	−17.896	30.864	15.619		144.08	H
ATOM	12472	HD3	ARG F	142	−17.595	32.419	15.461		144.08	H
ATOM	12473	HE	ARG F	142	−20.043	31.315	15.542		151.95	H
ATOM	12474	HH11	ARG F	142	−18.480	34.099	14.666		148.80	H
ATOM	12475	HH12	ARG F	142	−19.684	34.975	14.691		148.80	H
ATOM	12476	HH21	ARG F	142	−21.862	32.662	15.573		163.71	H
ATOM	12477	HH22	ARG F	142	−21.727	34.107	15.239		163.71	H
ATOM	12478	N	LYS F	143	−16.343	28.261	12.495		124.90	N
ATOM	12479	CA	LYS F	143	−17.016	27.049	12.034		128.02	C
ATOM	12480	C	LYS F	143	−16.646	25.854	12.897		128.44	C
ATOM	12481	O	LYS F	143	−17.509	25.084	13.314		128.33	O
ATOM	12482	CB	LYS F	143	−16.656	26.740	10.581		127.89	C
ATOM	12483	CG	LYS F	143	−17.165	27.743	9.576		121.75	C
ATOM	12484	CD	LYS F	143	−16.613	27.446	8.190		124.93	C
ATOM	12485	CE	LYS F	143	−17.698	26.971	7.242		133.41	C
ATOM	12486	NZ	LYS F	143	−18.262	25.655	7.631		138.22	N1+
ATOM	12487	H	LYS F	143	−15.826	28.619	11.908		129.88	H
ATOM	12488	HA	LYS F	143	−17.976	27.177	12.089		133.63	H
ATOM	12489	HB2	LYS F	143	−15.689	26.711	10.502		133.47	H
ATOM	12490	HB3	LYS F	143	−17.028	25.876	10.347		133.47	H
ATOM	12491	HG2	LYS F	143	−18.133	27.697	9.536		126.10	H
ATOM	12492	HG3	LYS F	143	−16.879	28.633	9.835		126.10	H
ATOM	12493	HD2	LYS F	143	−16.221	28.253	7.822		129.91	H
ATOM	12494	HD3	LYS F	143	−15.942	26.748	8.256		129.91	H
ATOM	12495	HE2	LYS F	143	−18.420	27.618	7.239		140.09	H
ATOM	12496	HE3	LYS F	143	−17.324	26.886	6.351		140.09	H
ATOM	12497	HZ1	LYS F	143	−17.620	25.038	7.635		145.86	H
ATOM	12498	HZ2	LYS F	143	−18.619	25.706	8.445		145.86	H
ATOM	12499	HZ3	LYS F	143	−18.893	25.412	7.052		145.86	H
ATOM	12500	N	MET F	144	−15.350	25.703	13.146		124.38	N
ATOM	12501	CA	MET F	144	−14.836	24.550	13.866		127.30	C
ATOM	12502	C	MET F	144	−15.415	24.490	15.276		134.88	C
ATOM	12503	O	MET F	144	−15.839	23.429	15.735		135.17	O
ATOM	12504	CB	MET F	144	−13.307	24.597	13.910		131.14	C
ATOM	12505	CG	MET F	144	−12.660	23.367	14.523		131.20	C
ATOM	12506	SD	MET F	144	−11.998	23.709	16.160		144.38	S
ATOM	12507	CE	MET F	144	−10.619	24.779	15.748		136.74	C
ATOM	12508	H	MET F	144	−14.743	26.263	12.906		129.26	H
ATOM	12509	HA	MET F	144	−15.093	23.745	13.389		132.76	H
ATOM	12510	HB2	MET F	144	−12.973	24.685	13.004		137.36	H
ATOM	12511	HB3	MET F	144	−13.035	25.365	14.435		137.36	H
ATOM	12512	HG2	MET F	144	−13.323	22.664	14.605		137.44	H
ATOM	12513	HG3	MET F	144	−11.930	23.074	13.955		137.44	H
ATOM	12514	HE1	MET F	144	−10.168	25.040	16.566		144.09	H
ATOM	12515	HE2	MET F	144	−10.007	24.296	15.172		144.09	H
ATOM	12516	HE3	MET F	144	−10.956	25.565	15.290		144.09	H
ATOM	12517	N	GLU F	145	−15.455	25.636	15.948		129.62	N
ATOM	12518	CA	GLU F	145	−15.954	25.704	17.316		135.30	C
ATOM	12519	C	GLU F	145	−17.462	25.475	17.409		133.13	C
ATOM	12520	O	GLU F	145	−17.954	24.977	18.420		134.65	O
ATOM	12521	CB	GLU F	145	−15.597	27.055	17.934		131.57	C
ATOM	12522	CG	GLU F	145	−14.112	27.209	18.208		133.34	C
ATOM	12523	CD	GLU F	145	−13.765	28.538	18.842		132.82	C
ATOM	12524	OE1	GLU F	145	−14.628	29.444	18.853		141.83	O
ATOM	12525	OE2	GLU F	145	−12.625	28.672	19.332		137.68	O1−
ATOM	12526	H	GLU F	145	−15.197	26.392	15.631		135.54	H
ATOM	12527	HA	GLU F	145	−15.518	25.015	17.841		142.36	H
ATOM	12528	HB2	GLU F	145	−15.864	27.760	17.324		137.89	H
ATOM	12529	HB3	GLU F	145	−16.069	27.150	18.776		137.89	H
ATOM	12530	HG2	GLU F	145	−13.828	26.506	18.813		140.00	H
ATOM	12531	HG3	GLU F	145	−13.628	27.142	17.370		140.00	H
ATOM	12532	N	ASP F	146	−18.190	25.837	16.359		133.24	N
ATOM	12533	CA	ASP F	146	−19.641	25.667	16.339		137.33	C
ATOM	12534	C	ASP F	146	−20.054	24.299	15.791		142.30	C
ATOM	12535	O	ASP F	146	−21.244	24.010	15.660		150.59	O
ATOM	12536	CB	ASP F	146	−20.292	26.776	15.510		134.15	C
ATOM	12537	CG	ASP F	146	−20.188	28.139	16.169		138.34	C
ATOM	12538	OD1	ASP F	146	−19.944	28.201	17.393		139.97	O
ATOM	12539	OD2	ASP F	146	−20.362	29.152	15.460		137.23	O1−
ATOM	12540	H	ASP F	146	−17.868	26.186	15.641		139.88	H
ATOM	12541	HA	ASP F	146	−19.976	25.737	17.247		144.79	H
ATOM	12542	HB2	ASP F	146	−19.853	26.825	14.647		140.97	H
ATOM	12543	HB3	ASP F	146	−21.233	26.570	15.393		140.97	H
ATOM	12544	N	SER F	147	−19.073	23.459	15.476		144.15	N
ATOM	12545	CA	SER F	147	−19.348	22.137	14.921		150.25	C
ATOM	12546	C	SER F	147	−20.056	21.244	15.935		151.65	C
ATOM	12547	O	SER F	147	−19.657	21.172	17.098		147.99	O
ATOM	12548	CB	SER F	147	−18.052	21.468	14.460		145.00	C
ATOM	12549	OG	SER F	147	−18.303	20.164	13.961		148.06	O
ATOM	12550	H	SER F	147	−18.236	23.631	15.575		152.98	H
ATOM	12551	HA	SER F	147	−19.928	22.233	14.149		160.30	H
ATOM	12552	HB2	SER F	147	−17.654	22.003	13.756		154.00	H
ATOM	12553	HB3	SER F	147	−17.444	21.406	15.213		154.00	H
ATOM	12554	HG	SER F	147	−17.584	19.809	13.712		157.67	H
ATOM	12555	N	LYS F	148	−21.095	20.552	15.474		156.81	N
ATOM	12556	CA	LYS F	148	−21.896	19.678	16.328		160.25	C
ATOM	12557	C	LYS F	148	−21.256	18.299	16.469		162.99	C
ATOM	12558	O	LYS F	148	−21.945	17.311	16.731		162.68	O
ATOM	12559	CB	LYS F	148	−23.312	19.528	15.761		156.25	C
ATOM	12560	CG	LYS F	148	−23.992	20.839	15.384		164.67	C
ATOM	12561	CD	LYS F	148	−25.039	21.247	16.406		171.20	C
ATOM	12562	CE	LYS F	148	−25.557	22.651	16.134		176.82	C
ATOM	12563	NZ	LYS F	148	−24.495	23.682	16.310		175.60	N1+
ATOM	12564	H	LYS F	148	−21.360	20.572	14.656		168.17	H
ATOM	12565	HA	LYS F	148	−21.964	20.071	17.211		172.30	H
ATOM	12566	HB2	LYS F	148	−23.268	18.980	14.962		167.50	H
ATOM	12567	HB3	LYS F	148	−23.866	19.091	16.426		167.50	H
ATOM	12568	HG2	LYS F	148	−23.325	21.542	15.336		177.61	H
ATOM	12569	HG3	LYS F	148	−24.431	20.736	14.525		177.61	H
ATOM	12570	HD2	LYS F	148	−25.788	20.632	16.361		185.44	H
ATOM	12571	HD3	LYS F	148	−24.645	21.234	17.292		185.44	H
ATOM	12572	HE2	LYS F	148	−25.877	22.701	15.219		192.19	H
ATOM	12573	HE3	LYS F	148	−26.277	22.850	16.752		192.19	H
ATOM	12574	HZ1	LYS F	148	−23.822	23.524	15.749		190.72	H
ATOM	12575	HZ2	LYS F	148	−24.826	24.491	16.145		190.72	H
ATOM	12576	HZ3	LYS F	148	−24.187	23.660	17.145		190.72	H
ATOM	12577	N	ARG F	149	−19.938	18.236	16.295		162.51	N
ATOM	12578	CA	ARG F	149	−19.219	16.968	16.305		165.70	C
ATOM	12579	C	ARG F	149	−17.746	17.180	16.640		170.51	C
ATOM	12580	O	ARG F	149	−17.410	17.671	17.718		179.82	O
ATOM	12581	CB	ARG F	149	−19.361	16.277	14.948		159.09	C
ATOM	12582	CG	ARG F	149	−18.637	14.951	14.834		153.79	C
ATOM	12583	CD	ARG F	149	−18.960	14.289	13.514		143.18	C
ATOM	12584	NE	ARG F	149	−18.021	13.226	13.181		143.60	N
ATOM	12585	CZ	ARG F	149	−18.019	12.580	12.021		140.65	C
ATOM	12586	NH1	ARG F	149	−18.915	12.894	11.095		130.30	N1+
ATOM	12587	NH2	ARG F	149	−17.125	11.627	11.791		140.71	N
ATOM	12588	H	ARG F	149	−19.434	18.921	16.169		175.01	H
ATOM	12589	HA	ARG F	149	−19.603	16.389	16.982		178.85	H
ATOM	12590	HB2	ARG F	149	−20.303	16.112	14.782		170.91	H
ATOM	12591	HB3	ARG F	149	−19.007	16.865	14.263		170.91	H
ATOM	12592	HG2	ARG F	149	−17.679	15.101	14.877		164.55	H
ATOM	12593	HG3	ARG F	149	−18.921	14.363	15.551		164.55	H
ATOM	12594	HD2	ARG F	149	−19.848	13.902	13.562		151.81	H
ATOM	12595	HD3	ARG F	149	−18.925	14.954	12.808		151.81	H
ATOM	12596	HE	ARG F	149	−17.372	13.078	13.725		152.32	H
ATOM	12597	HH11	ARG F	149	−19.492	13.514	11.246		136.36	H
ATOM	12598	HH12	ARG F	149	−18.919	12.478	10.342		136.36	H
ATOM	12599	HH21	ARG F	149	−16.546	11.425	12.394		148.86	H
ATOM	12600	HH22	ARG F	149	−17.127	11.207	11.040		148.86	H

Claims (5)

What is claimed is:

1. A method of expanding cytotoxic lymphocytes ex vivo, comprising culturing a population of lymphocytes in the presence of a chimeric peptide,

wherein the chimeric peptide comprises an orthopoxvirus major histocompatibility complex class 1-like protein (OMCP) peptide linked to an interleukin-2 (IL-2) mutant peptide comprising the amino acid sequence of SEQ ID NO: 5 comprising at least one mutation, wherein the at least one mutation is R38A, F42K, or C125S relative to SEQ ID NO: 5 wherein the OMCP peptide comprises an amino acid sequence selected from the group consisting of SEQ ID NO: 7, SEQ ID NO: 13, and SEQ ID NO: 14, and

wherein the population of lymphocytes comprises cytotoxic lymphocytes.

2. The method of claim 1, wherein the OMCP peptide comprises the amino acid sequence of SEQ ID NO: 7.

3. The method of claim 1, wherein the OMCP peptide comprises the amino acid sequence of SEQ ID NO: 13.

4. The method of claim 3, wherein the OMCP peptide comprises the amino acid sequence of SEQ ID NO: 14.

5. The method of claim 1, wherein the cytotoxic lymphocytes comprise CD8+ T cells and/or NK cells.

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